{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T08:25:00Z","timestamp":1787646300717,"version":"build-2736575974"},"reference-count":86,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T00:00:00Z","timestamp":1780272000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,6,1]],"date-time":"2026-06-01T00:00:00Z","timestamp":1780272000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,5,2]],"date-time":"2026-05-02T00:00:00Z","timestamp":1777680000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Key Research and Development Program of China","doi-asserted-by":"publisher","award":["2025YFA0921300"],"award-info":[{"award-number":["2025YFA0921300"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32025001"],"award-info":[{"award-number":["32025001"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32571464"],"award-info":[{"award-number":["32571464"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014103","name":"Key Technology Research and Development Program of Shandong Province","doi-asserted-by":"publisher","award":["2025TSGCCZZB0768"],"award-info":[{"award-number":["2025TSGCCZZB0768"]}],"id":[{"id":"10.13039\/100014103","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,6]]},"DOI":"10.1016\/j.jbc.2026.113116","type":"journal-article","created":{"date-parts":[[2026,5,7]],"date-time":"2026-05-07T06:52:28Z","timestamp":1778136748000},"page":"113116","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Supporting activities of cognate redox partners for sterol-metabolizing P450 enzymes in Mycobacterium neoaurum"],"prefix":"10.1016","volume":"302","author":[{"given":"Yunjie","family":"Liu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yue","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weihan","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nian","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunjun","family":"Pan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1601-7125","authenticated-orcid":false,"given":"Li","family":"Ma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5244-870X","authenticated-orcid":false,"given":"Shengying","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113116_bib1","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2021.107860","article-title":"Mycolicibacterium cell factory for the production of steroid-based drug intermediates","volume":"53","author":"Zhao","year":"2021","journal-title":"Biotechnol. Adv."},{"key":"10.1016\/j.jbc.2026.113116_bib2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12934-020-01335-y","article-title":"Enhancing the bioconversion of phytosterols to steroidal intermediates by the deficiency of kasb in the cell wall synthesis of mycobacterium neoaurum","volume":"19","author":"Xiong","year":"2020","journal-title":"Microb. Cell Fact."},{"key":"10.1016\/j.jbc.2026.113116_bib3","doi-asserted-by":"crossref","first-page":"5474","DOI":"10.1002\/ange.202015462","article-title":"A dual role reductase from phytosterols catabolism enables the efficient production of valuable steroid precursors","volume":"133","author":"Peng","year":"2021","journal-title":"Angew. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib4","doi-asserted-by":"crossref","first-page":"958","DOI":"10.3389\/fmicb.2018.00958","article-title":"New insights on steroid biotechnology","volume":"9","author":"Fern\u00e1ndez-Cabez\u00f3n","year":"2018","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2026.113116_bib5","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1007\/s00253-012-4078-0","article-title":"Microbial steroid transformations: current state and prospects","volume":"94","author":"Donova","year":"2012","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib6","doi-asserted-by":"crossref","first-page":"3349","DOI":"10.1021\/ja01869a023","article-title":"The preparation of trillin and its conversion to progesterone","volume":"62","author":"Marker","year":"1940","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2026.113116_bib7","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.ymben.2019.10.006","article-title":"Identification of absidia orchidis steroid 11\u03b2-hydroxylation system and its application in engineering saccharomyces cerevisiae for one-step biotransformation to produce hydrocortisone","volume":"57","author":"Chen","year":"2020","journal-title":"Metab. Eng."},{"key":"10.1016\/j.jbc.2026.113116_bib8","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.plipres.2013.03.001","article-title":"Yeast metabolic engineering\u2013targeting sterol metabolism and terpenoid formation","volume":"52","author":"Wriessnegger","year":"2013","journal-title":"Prog. Lipid Res."},{"key":"10.1016\/j.jbc.2026.113116_bib9","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/nbt0298-186","article-title":"Self-sufficient biosynthesis of pregnenolone and progesterone in engineered yeast","volume":"16","author":"Duport","year":"1998","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib10","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1016\/j.biortech.2006.10.006","article-title":"Phytosterols: applications and recovery methods","volume":"98","author":"Fernandes","year":"2007","journal-title":"Bioresour. Technol."},{"key":"10.1016\/j.jbc.2026.113116_bib11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12896-019-0533-7","article-title":"Genome-wide response on phytosterol in 9-hydroxyandrostenedione-producing strain of mycobacterium sp. VKM Ac-1817d","volume":"19","author":"Bragin","year":"2019","journal-title":"BMC Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib12","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1111\/1751-7915.12429","article-title":"Mycobacterium smegmatis is a suitable cell factory for the production of steroidic synthons","volume":"10","author":"Galan","year":"2017","journal-title":"Microb. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib13","article-title":"Identification of the aldolase responsible for the production of 22-hydroxy-23, 24-bisnorchol-4-ene-3-one from natural sterols in mycolicibacterium smegmatis","volume":"17","author":"Hern\u00e1ndez Fern\u00e1ndez","year":"2024","journal-title":"Microb. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib14","doi-asserted-by":"crossref","first-page":"598","DOI":"10.3390\/molecules21050598","article-title":"The role of fadd19 and echa19 in sterol side chain degradation bymycobacterium smegmatis","volume":"21","author":"Wro\u0144ska","year":"2016","journal-title":"Molecules"},{"key":"10.1016\/j.jbc.2026.113116_bib15","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.ymben.2012.10.005","article-title":"Identification and engineering of cholesterol oxidases involved in the initial step of sterols catabolism in mycobacterium neoaurum","volume":"15","author":"Yao","year":"2013","journal-title":"Metab. Eng."},{"key":"10.1016\/j.jbc.2026.113116_bib16","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.jsbmb.2011.09.008","article-title":"Cholesterol oxidase ChoD is not a critical enzyme accounting for oxidation of sterols to 3-keto-4-ene steroids in fast-growing mycobacterium sp. VKM Ac-1815d","volume":"129","author":"Ivashina","year":"2012","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113116_bib17","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.micres.2010.05.003","article-title":"ChoG is the main inducible extracellular cholesterol oxidase of rhodococcus sp. Strain Cect3014","volume":"166","author":"de Las Heras","year":"2011","journal-title":"Microbiol. Res."},{"key":"10.1016\/j.jbc.2026.113116_bib18","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2024.107243","article-title":"Bacterial stigmasterol degradation involving radical flavin delta-24 desaturase and molybdenum-dependent c26 hydroxylase","volume":"300","author":"Zhan","year":"2024","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib19","doi-asserted-by":"crossref","DOI":"10.1016\/j.jsbmb.2023.106317","article-title":"The oxidation of cholesterol derivatives by the CYP124 and CYP142 enzymes from mycobacterium marinum","volume":"231","author":"Ghith","year":"2023","journal-title":"J. Steroid. Biochem. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113116_bib20","doi-asserted-by":"crossref","DOI":"10.1016\/j.jsbmb.2023.106406","article-title":"The oxidation of steroid derivatives by the CYP125a6 and CYP125a7 enzymes from mycobacterium marinum","volume":"235","author":"Ghith","year":"2023","journal-title":"J. Steroid. Biochem. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113116_bib21","doi-asserted-by":"crossref","DOI":"10.1002\/chem.202203868","article-title":"Structure based discovery of inhibitors of CYP125 and CYP142 from mycobacterium Tuberculosis","volume":"29","author":"Katariya","year":"2023","journal-title":"Chem. Eur. J."},{"key":"10.1016\/j.jbc.2026.113116_bib22","doi-asserted-by":"crossref","first-page":"9392","DOI":"10.1039\/D3CC02312E","article-title":"The bacterial cytochrome p450 (CYP) CYP125 enzymes can competitively oxidise sitosterol in the presence of cholesterol","volume":"59","author":"Doherty","year":"2023","journal-title":"Chem. Commun."},{"key":"10.1016\/j.jbc.2026.113116_bib23","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1111\/j.1365-2958.2010.07243.x","article-title":"Mycobacterium tuberculosis CYP125a1, a steroid c27 monooxygenase that detoxifies intracellularly generated cholest-4-en-3-one","volume":"77","author":"Ouellet","year":"2010","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.113116_bib24","doi-asserted-by":"crossref","first-page":"35534","DOI":"10.1074\/jbc.M109.072132","article-title":"Mycobacterial cytochrome p450 125 (cyp125) catalyzes the terminal hydroxylation of c27 steroids","volume":"284","author":"Capyk","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib25","article-title":"Unraveling and engineering the production of 23, 24-bisnorcholenic steroids in sterol metabolism","volume":"6","author":"Xu","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2026.113116_bib26","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1021\/id500033m","article-title":"Unraveling cholesterol catabolism in mycobacterium tuberculosis: ChsE4-ChsE5 \u03b12\u03b22 acyl-CoA dehydrogenase initiates \u03b2-oxidation of 3-oxo-cholest-4-en-26-oyl CoA","volume":"1","author":"Yang","year":"2015","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.jbc.2026.113116_bib27","doi-asserted-by":"crossref","first-page":"4455","DOI":"10.1128\/AEM.00380-11","article-title":"FadD19 of rhodococcus rhodochrous DSM43269, a steroid-coenzyme a ligase essential for degradation of c-24 branched sterol side chains","volume":"77","author":"Wilbrink","year":"2011","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.jbc.2026.113116_bib28","doi-asserted-by":"crossref","first-page":"1947","DOI":"10.1073\/pnas.0605728104","article-title":"A gene cluster encoding cholesterol catabolism in a soil actinomycete provides insight into mycobacterium tuberculosis survival in macrophages","volume":"104","author":"Van der Geize","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113116_bib29","doi-asserted-by":"crossref","first-page":"1072","DOI":"10.1039\/D1NP00004G","article-title":"Cytochrome p450 enzymes in fungal natural product biosynthesis","volume":"38","author":"Zhang","year":"2021","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.jbc.2026.113116_bib30","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.cbpa.2016.02.018","article-title":"Applications of microbial cytochrome p450 enzymes in biotechnology and synthetic biology","volume":"31","author":"Girvan","year":"2016","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.jbc.2026.113116_bib31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.pharmtox.45.120403.100030","article-title":"Cytochrome p450: nature's most versatile biological catalyst","volume":"45","author":"Coon","year":"2005","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.jbc.2026.113116_bib32","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1039\/C7NP00028F","article-title":"Expansion of chemical space for natural products by uncommon p450 reactions","volume":"34","author":"Zhang","year":"2017","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.jbc.2026.113116_bib33","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1039\/C7NP00034K","article-title":"Cytochromes p450 for natural product biosynthesis in streptomyces: sequence, structure, and function","volume":"34","author":"Rudolf","year":"2017","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.jbc.2026.113116_bib34","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1039\/c2np20020a","article-title":"Diversity of p450 enzymes in the biosynthesis of natural products","volume":"29","author":"Podust","year":"2012","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.jbc.2026.113116_bib35","doi-asserted-by":"crossref","first-page":"5736","DOI":"10.1074\/jbc.M110.204420","article-title":"Structural characterization of the complex between \u03b1-naphthoflavone and human cytochrome p450 1b1","volume":"286","author":"Wang","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib36","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1021\/tx0002583","article-title":"Common and uncommon cytochrome p450 reactions related to metabolism and chemical toxicity","volume":"14","author":"Guengerich","year":"2001","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.jbc.2026.113116_bib37","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.tim.2020.02.012","article-title":"Redox partners: function modulators of bacterial p450 enzymes","volume":"28","author":"Li","year":"2020","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.jbc.2026.113116_bib38","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/j.bbagen.2006.07.017","article-title":"Cytochrome p450 systems\u2014biological variations of electron transport chains","volume":"1770","author":"Hannemann","year":"2007","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.jbc.2026.113116_bib39","doi-asserted-by":"crossref","first-page":"2815","DOI":"10.1002\/bit.24960","article-title":"Semi-rational engineering of cytochrome p450sca-2 in a hybrid system for enhanced catalytic activity: insights into the important role of electron transfer","volume":"110","author":"Ba","year":"2013","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.jbc.2026.113116_bib40","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.3762\/bjoc.7.173","article-title":"Chimeric self-sufficient p450cam-RhFRed biocatalysts with broad substrate scope","volume":"7","author":"Robin","year":"2011","journal-title":"Beilstein J. Org. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib41","doi-asserted-by":"crossref","first-page":"12940","DOI":"10.1021\/ja075842d","article-title":"Engineering and analysis of a self-sufficient biosynthetic cytochrome p450 PikC fused to the RhFRED reductase domain","volume":"129","author":"Li","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2026.113116_bib42","doi-asserted-by":"crossref","DOI":"10.1098\/rstb.2012.0434","article-title":"Unusual properties of the cytochrome p450 superfamily","volume":"368","author":"Lamb","year":"2013","journal-title":"Philos. Trans. R. Soc. B Biol. Sci."},{"key":"10.1016\/j.jbc.2026.113116_bib43","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1007\/s00203-008-0438-7","article-title":"Functional characterisation of the peroxiredoxin gene family members of synechococcus elongatus PCC 7942","volume":"191","author":"Stork","year":"2009","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.jbc.2026.113116_bib44","doi-asserted-by":"crossref","first-page":"17486","DOI":"10.1074\/jbc.M700863200","article-title":"Electron transport pathway for a streptomyces cytochrome p450: cytochrome p450 105d5-catalyzed fatty acid hydroxylation in streptomyces coelicolor a3 (2)","volume":"282","author":"Chun","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib45","doi-asserted-by":"crossref","first-page":"4366","DOI":"10.1021\/cr400479b","article-title":"Metalloproteins containing cytochrome, iron\u2013sulfur, or copper redox centers","volume":"114","author":"Liu","year":"2014","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2026.113116_bib46","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/s00775-007-0318-7","article-title":"Iron\u2013sulfur protein folds, iron\u2013sulfur chemistry, and evolution","volume":"13","author":"Meyer","year":"2008","journal-title":"J. Biol. Inorg. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib47","doi-asserted-by":"crossref","first-page":"4161","DOI":"10.3390\/ijms24044161","article-title":"Evolution of cytochrome p450 enzymes and their redox partners in Archaea","volume":"24","author":"Ngcobo","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.113116_bib48","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1038\/s42003-022-03764-4","article-title":"Three pairs of surrogate redox partners comparison for class i cytochrome p450 enzyme activity reconstitution","volume":"5","author":"Liu","year":"2022","journal-title":"Commun. Biol."},{"key":"10.1016\/j.jbc.2026.113116_bib49","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1093\/molbev\/msaa260","article-title":"Concerning p450 evolution: structural analyses support bacterial origin of sterol 14\u03b1-demethylases","volume":"38","author":"Lamb","year":"2021","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.jbc.2026.113116_bib50","doi-asserted-by":"crossref","first-page":"9992","DOI":"10.1021\/acscatal.8b02913","article-title":"Mechanistic insights into interactions between bacterial class i p450 enzymes and redox partners","volume":"8","author":"Zhang","year":"2018","journal-title":"ACS Catal."},{"key":"10.1016\/j.jbc.2026.113116_bib51","doi-asserted-by":"crossref","unstructured":"D.R. Nelson, Cytochrome p450 Nomenclature, 2004, In: Cytochrome P450 Protocol. 2nd Ed., (Phillips, I. R., and Shephard, E. A., eds). Methods in Molecular Biology, 320, 2006, Humana Press; Totowa, NJ, 1\u201310.","DOI":"10.1385\/1-59259-998-2:1"},{"key":"10.1016\/j.jbc.2026.113116_bib52","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1042\/BST20170218","article-title":"Structure and function of the cytochrome p450 peroxygenase enzymes","volume":"46","author":"Munro","year":"2018","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jbc.2026.113116_bib53","doi-asserted-by":"crossref","first-page":"18481","DOI":"10.1021\/acsomega.2c00960","article-title":"Structural insights on the conversion of cytochrome p450 to p420","volume":"7","author":"Gable","year":"2022","journal-title":"ACS Omega"},{"key":"10.1016\/j.jbc.2026.113116_bib54","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1038\/nbt0897-784","article-title":"Drug metabolism by escherichia coli expressing human cytochromes p450","volume":"15","author":"Parikh","year":"1997","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib55","doi-asserted-by":"crossref","first-page":"6148","DOI":"10.3390\/ijms24076148","article-title":"Whole-genome analysis of mycobacterium neoaurum DSM 1381 and the validation of two key enzymes affecting c22 steroid intermediates in sterol metabolism","volume":"24","author":"Zhang","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2026.113116_bib56","doi-asserted-by":"crossref","first-page":"e00420","DOI":"10.1128\/AEM.00441-20","article-title":"The sterol carrier hydroxypropyl-\u03b2-cyclodextrin enhances the metabolism of phytosterols by mycobacterium neoaurum","volume":"86","author":"Su","year":"2020","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.jbc.2026.113116_bib57","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/j.ymben.2019.09.004","article-title":"Characterization and engineering control of the effects of reactive oxygen species on the conversion of sterols to steroid synthons in mycobacterium neoaurum","volume":"56","author":"Sun","year":"2019","journal-title":"Metab. Eng."},{"key":"10.1016\/j.jbc.2026.113116_bib58","doi-asserted-by":"crossref","first-page":"12141","DOI":"10.1021\/acs.jafc.8b04777","article-title":"Metabolic adaptation of mycobacterium neoaurum ATCC 25795 in the catabolism of sterols for producing important steroid intermediates","volume":"66","author":"Liu","year":"2018","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib59","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.steroids.2018.02.001","article-title":"New product identification in the sterol metabolism by an industrial strain mycobacterium neoaurum NRRL b-3805","volume":"132","author":"Li","year":"2018","journal-title":"Steroids"},{"key":"10.1016\/j.jbc.2026.113116_bib60","doi-asserted-by":"crossref","first-page":"6909","DOI":"10.1021\/acs.biochem.5b01029","article-title":"Cytochrome p450 125a4, the third cholesterol c-26 hydroxylase from mycobacterium smegmatis","volume":"54","author":"Frank","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113116_bib61","doi-asserted-by":"crossref","first-page":"36352","DOI":"10.1074\/jbc.M110.161117","article-title":"Functional redundancy of steroid c26-monooxygenase activity in mycobacterium tuberculosis revealed by biochemical and genetic analyses","volume":"285","author":"Johnston","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib62","doi-asserted-by":"crossref","first-page":"10472","DOI":"10.1074\/jbc.275.14.10472","article-title":"Competition between c-terminal tyrosine and nicotinamide modulates pyridine nucleotide affinity and specificity in plant ferredoxin-NADP(+) reductase","volume":"275","author":"Piubelli","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib63","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1006\/jmbi.2000.4042","article-title":"T-coffee: a novel method for fast and accurate multiple sequence alignment","volume":"302","author":"Notredame","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113116_bib64","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1111\/j.1742-4658.2009.06974.x","article-title":"A novel electron transport system for thermostable CYP175a1 from thermus thermophilus HB27","volume":"276","author":"Mandai","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2026.113116_bib65","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1007\/s43393-023-00161-8","article-title":"The function of steroid terminal monooxygenase in cholesterol or phytosterol degradation by the mycobacterium neoaurum NRRL b-3805","volume":"3","author":"Li","year":"2023","journal-title":"Sys. Microbiol. Biomanuf."},{"key":"10.1016\/j.jbc.2026.113116_bib66","first-page":"530","article-title":"Cholesterol catabolism as a therapeutic target in mycobacterium tuberculosis Trends Microbiol","volume":"19","author":"Ouellet","year":"2011"},{"key":"10.1016\/j.jbc.2026.113116_bib67","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1002\/bab.1087","article-title":"Novel family members of CYP109 from sorangium cellulosum soce 56 exhibit characteristic biochemical and biophysical properties","volume":"60","author":"Khatri","year":"2013","journal-title":"Biotechnol. Appl. Biochem."},{"key":"10.1016\/j.jbc.2026.113116_bib68","doi-asserted-by":"crossref","first-page":"5723","DOI":"10.1074\/jbc.M807592200","article-title":"Analysis of transient and catalytic desosamine-binding pockets in cytochrome p450 PikC from streptomyces venezuelae","volume":"284","author":"Li","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib71","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1089\/ars.2017.7216","article-title":"NAD(h) and NADP(h) redox couples and cellular energy metabolism","volume":"28","author":"Xiao","year":"2018","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.jbc.2026.113116_bib72","doi-asserted-by":"crossref","first-page":"742","DOI":"10.3389\/fmicb.2015.00742","article-title":"NADPH-generating systems in bacteria and archaea","volume":"6","author":"Spaans","year":"2015","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2026.113116_bib69","doi-asserted-by":"crossref","first-page":"13193","DOI":"10.1021\/jacs.7b07656","article-title":"Effect of redox partner binding on cytochrome p450 conformational dynamics","volume":"139","author":"Batabyal","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2026.113116_bib70","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.abb.2010.08.022","article-title":"Structural biology of redox partner interactions in p450cam monooxygenase: a fresh look at an old system","volume":"507","author":"Sevrioukova","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jbc.2026.113116_bib73","doi-asserted-by":"crossref","first-page":"4353","DOI":"10.1016\/j.jmb.2013.07.006","article-title":"The structure of the cytochrome p450cam\u2013putidaredoxin complex determined by paramagnetic NMR spectroscopy and crystallography","volume":"425","author":"Hiruma","year":"2013","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113116_bib74","doi-asserted-by":"crossref","first-page":"100794","DOI":"10.1016\/j.jbc.2021.100794","article-title":"Structural and functional insights into aldosterone synthase interaction with its redox partner protein adrenodoxin","volume":"296","author":"Brixius-Anderko","year":"2021","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib75","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.tibtech.2011.06.012","article-title":"Cytochrome p450 monooxygenases: an update on perspectives for synthetic application","volume":"30","author":"Urlacher","year":"2012","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib76","doi-asserted-by":"crossref","first-page":"6185","DOI":"10.1007\/s00253-014-5767-7","article-title":"Cytochromes p450 as promising catalysts for biotechnological application: chances and limitations","volume":"98","author":"Bernhardt","year":"2014","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib77","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.copbio.2016.05.005","article-title":"Recent advances in whole cell biocatalysis techniques bridging from investigative to industrial scale","volume":"42","author":"Wachtmeister","year":"2016","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib78","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2024.1343029","article-title":"Bacterial cytochrome p450s: a bioinformatics odyssey of substrate discovery","volume":"15","author":"Schottlender","year":"2024","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2026.113116_bib79","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1021\/acs.accounts.1c00632","article-title":"Updating the paradigm: redox partner binding and conformational dynamics in cytochromes p450","volume":"55","author":"Poulos","year":"2021","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.jbc.2026.113116_bib80","doi-asserted-by":"crossref","first-page":"14563","DOI":"10.1021\/acs.joc.1c01407","article-title":"Bacterial biosynthetic p450 enzyme PikCD50n: a potential biocatalyst for the preparation of human drug metabolites","volume":"86","author":"Guo","year":"2021","journal-title":"J. Org. Chem."},{"key":"10.1016\/j.jbc.2026.113116_bib81","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/S1074-5521(98)90293-9","article-title":"Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikc-encoded cytochrome p450 in streptomyces venezuelae","volume":"5","author":"Xue","year":"1998","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jbc.2026.113116_bib82","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.bbapap.2003.12.005","article-title":"Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP (h) reductases","volume":"1698","author":"Ceccarelli","year":"2004","journal-title":"BBA-Proteins Proteomics"},{"key":"10.1016\/j.jbc.2026.113116_bib83","doi-asserted-by":"crossref","first-page":"10417","DOI":"10.1007\/s00253-016-7704-4","article-title":"A novel NADPH-dependent reductase of sulfobacillus acidophilus TPY phenol hydroxylase: expression, characterization, and functional analysis","volume":"100","author":"Li","year":"2016","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbc.2026.113116_bib84","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1046\/j.1432-1033.2003.03566.x","article-title":"Open questions in ferredoxin-NADP+ reductase catalytic mechanism","volume":"270","author":"Carrillo","year":"2003","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2026.113116_bib85","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1002\/prot.22510","article-title":"Crystal structure of a ferredoxin reductase for the CYP199a2 system from rhodopseudomonas palustris","volume":"77","author":"Xu","year":"2009","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2026.113116_bib86","doi-asserted-by":"crossref","first-page":"253","DOI":"10.11613\/BM.2017.026","article-title":"Resolution of students t-tests, ANOVA and analysis of variance components from intermediary data","volume":"27","author":"Kallner","year":"2017","journal-title":"Biochem. Med."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826019885?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826019885?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,25]],"date-time":"2026-08-25T07:28:06Z","timestamp":1787642886000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826019885"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6]]},"references-count":86,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2026,6]]}},"alternative-id":["S0021925826019885"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113116","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Supporting activities of cognate redox partners for sterol-metabolizing P450 enzymes in Mycobacterium neoaurum","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113116","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"113116"}}