{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,16]],"date-time":"2026-10-16T17:42:50Z","timestamp":1792172570015,"version":"4.4.0"},"reference-count":67,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2022,4,26]],"date-time":"2022-04-26T00:00:00Z","timestamp":1650931200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000199","name":"United States Department of Agriculture","doi-asserted-by":"publisher","award":["USDA-ARS 6026-51000-012-06S"],"award-info":[{"award-number":["USDA-ARS 6026-51000-012-06S"]}],"id":[{"id":"10.13039\/100000199","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Sturgis Foundation Pilot Grant","award":["G1-54750-01"],"award-info":[{"award-number":["G1-54750-01"]}]},{"name":"ACRI-ABI Investigator Initiated grant Award","award":["GR037175-4450S ABI"],"award-info":[{"award-number":["GR037175-4450S ABI"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Myoglobin (Mb)-mediated oxygen (O2) delivery and dissolved O2 in the cytosol are two major sources that support oxidative phosphorylation. During intense exercise, lactate (LAC) production is elevated in skeletal muscles as a consequence of insufficient intracellular O2 supply. The latter results in diminished mitochondrial oxidative metabolism and an increased reliance on nonoxidative pathways to generate ATP. Whether or not metabolites from these pathways impact Mb-O2 associations remains to be established. In the present study, we employed isothermal titration calorimetry, O2 kinetic studies, and UV-Vis spectroscopy to evaluate the LAC affinity toward Mb (oxy- and deoxy-Mb) and the effect of LAC on O2 release from oxy-Mb in varying pH conditions (pH 6.0\u20137.0). Our results show that LAC avidly binds to both oxy- and deoxy-Mb (only at acidic pH for the latter). Similarly, in the presence of LAC, increased release of O2 from oxy-Mb was detected. This suggests that with LAC binding to Mb, the structural conformation of the protein (near the heme center) might be altered, which concomitantly triggers the release of O2. Taken together, these novel findings support a mechanism where LAC acts as a regulator of O2 management in Mb-rich tissues and\/or influences the putative signaling roles for oxy- and deoxy-Mb, especially under conditions of LAC accumulation and lactic acidosis.<\/jats:p>","DOI":"10.3390\/ijms23094747","type":"journal-article","created":{"date-parts":[[2022,4,26]],"date-time":"2022-04-26T02:14:39Z","timestamp":1650939279000},"page":"4747","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Myoglobin Interaction with Lactate Rapidly Releases Oxygen: Studies on Binding Thermodynamics, Spectroscopy, and Oxygen Kinetics"],"prefix":"10.3390","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6612-1823","authenticated-orcid":false,"given":"Kiran Kumar","family":"Adepu","sequence":"first","affiliation":[{"name":"Arkansas Children\u2019s Nutrition Center, Little Rock, AR 72202, USA"},{"name":"Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock, AR 72202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dipendra","family":"Bhandari","sequence":"additional","affiliation":[{"name":"Arkansas Children\u2019s Nutrition Center, Little Rock, AR 72202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andriy","family":"Anishkin","sequence":"additional","affiliation":[{"name":"Department of Biology, University of Maryland, College Park, MD 20742, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sean H.","family":"Adams","sequence":"additional","affiliation":[{"name":"Department of Surgery, School of Medicine, University of California, Davis, CA 95616, USA"},{"name":"Center for Alimentary and Metabolic Science, University of California, Davis, CA 95616, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8457-9643","authenticated-orcid":false,"given":"Sree V.","family":"Chintapalli","sequence":"additional","affiliation":[{"name":"Arkansas Children\u2019s Nutrition Center, Little Rock, AR 72202, USA"},{"name":"Department of Pediatrics, University of Arkansas for Medical Sciences, Little Rock, AR 72202, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,4,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1111\/j.1469-7793.1999.0633s.x","article-title":"Lactate transport in skeletal muscle\u2014role and regulation of the monocarboxylate transporter","volume":"517","author":"Juel","year":"1999","journal-title":"J. Physiol."},{"key":"ref_2","unstructured":"Voet, D., Voet, J.G., and Pratt, C.W. (2016). Fundamentals of Biochemistry Life at the Molecular Level, Wiley."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/j.cmet.2018.03.008","article-title":"The Science and Translation of Lactate Shuttle Theory","volume":"27","author":"Brooks","year":"2018","journal-title":"Cell Metab."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1038\/s42255-020-0243-4","article-title":"Lactate: The ugly duckling of energy metabolism","volume":"2","author":"Rabinowitz","year":"2020","journal-title":"Nat. Metab."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"101454","DOI":"10.1016\/j.redox.2020.101454","article-title":"Lactate as a fulcrum of metabolism","volume":"35","author":"Brooks","year":"2020","journal-title":"Redox Biol."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Proia, P., Di Liegro, C.M., Schiera, G., Fricano, A., and Di Liegro, I. (2016). Lactate as a Metabolite and a Regulator in the Central Nervous System. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17091450"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"E366","DOI":"10.1152\/ajpendo.00363.2006","article-title":"Pyruvate metabolism in working human skeletal muscle","volume":"292","author":"Henderson","year":"2007","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"22","DOI":"10.3389\/fnins.2015.00022","article-title":"Lactate is always the end product of glycolysis","volume":"9","author":"Rogatzki","year":"2015","journal-title":"Front. Neurosci."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"3550","DOI":"10.1038\/ncomms4550","article-title":"Acidosis overrides oxygen deprivation to maintain mitochondrial function and cell survival","volume":"5","author":"Khacho","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1249\/00005768-198502000-00003","article-title":"Anaerobic threshold: Review of the concept and directions for future research","volume":"17","author":"Davis","year":"1985","journal-title":"Med. Sci. Sports Exerc."},{"key":"ref_11","unstructured":"Foucher, C.D., and Tubben, R.E. (2021). Lactic Acidosis. StatPearls, StatPearls Publishing."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"S15","DOI":"10.1681\/ASN.V12suppl_1s15","article-title":"Lactic acidosis update for critical care clinicians","volume":"12","author":"Luft","year":"2001","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_13","unstructured":"Nelson, D.L., and Cox, M.M. (2017). Lehninger Principles of Biochemistry, W.H. Freeman. [7th ed.]."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1161\/01.CIR.63.6.1273","article-title":"Myocardial lactate metabolism: Evidence of lactate release during net chemical extraction in man","volume":"63","author":"Gertz","year":"1981","journal-title":"Circulation"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/j.jacbts.2016.06.009","article-title":"Evidence of Glycolysis Up-Regulation and Pyruvate Mitochondrial Oxidation Mismatch During Mechanical Unloading of the Failing Human Heart: Implications for Cardiac Reloading and Conditioning","volume":"1","author":"Diakos","year":"2016","journal-title":"JACC Basic Transl. Sci."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2190","DOI":"10.1161\/01.CIR.96.7.2190","article-title":"Myocardial phosphocreatine-to-ATP ratio is a predictor of mortality in patients with dilated cardiomyopathy","volume":"96","author":"Neubauer","year":"1997","journal-title":"Circulation"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"9038","DOI":"10.1016\/S0021-9258(19)40690-X","article-title":"Role of myoglobin in the oxygen supply to red skeletal muscle","volume":"250","author":"Wittenberg","year":"1975","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0034-5687(83)90012-9","article-title":"Skeletal muscle function in hypoxia: Effect of alteration of intracellular myoglobin","volume":"53","author":"Cole","year":"1983","journal-title":"Respir. Physiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/0300-9629(83)90451-6","article-title":"The fish heart as a model system for the study of myoglobin","volume":"76","author":"Driedzic","year":"1983","journal-title":"Comp. Biochem. Physiol. A Comp. Physiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/0034-5687(86)90095-2","article-title":"Myoglobin-dependent oxidative metabolism in the hypoxic rat heart","volume":"63","author":"Taylor","year":"1986","journal-title":"Respir. Physiol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"7503","DOI":"10.1073\/pnas.84.21.7503","article-title":"Myoglobin-mediated oxygen delivery to mitochondria of isolated cardiac myocytes","volume":"84","author":"Wittenberg","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1016\/j.bbadis.2009.06.005","article-title":"Myoglobin causes oxidative stress, increase of NO production and dysfunction of kidney\u2019s mitochondria","volume":"1792","author":"Plotnikov","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.niox.2019.06.001","article-title":"Compensatory mechanisms in myoglobin deficient mice preserve NO homeostasis","volume":"90","author":"Park","year":"2019","journal-title":"Nitric. Oxide"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/0304-4165(95)00161-1","article-title":"Conversion of metmyoglobin to NO myoglobin in the presence of nitrite and reductants","volume":"1289","author":"Nakamura","year":"1996","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"6976","DOI":"10.1021\/bi960442g","article-title":"Mechanism of NO-induced oxidation of myoglobin and hemoglobin","volume":"35","author":"Eich","year":"1996","journal-title":"Biochemistry"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1021\/cr000078y","article-title":"Nitric oxide and myoglobins","volume":"102","author":"Moller","year":"2002","journal-title":"Chem. Rev."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1038\/454416a","article-title":"Physiology: Myoglobin\u2019s new clothes","volume":"454","author":"Cossins","year":"2008","journal-title":"Nature"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.abb.2018.07.024","article-title":"Exploring the entry route of palmitic acid and palmitoylcarnitine into myoglobin","volume":"655","author":"Chintapalli","year":"2018","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Chintapalli, S.V., Bhardwaj, G., Patel, R., Shah, N., Patterson, R.L., van Rossum, D.B., Anishkin, A., and Adams, S.H. (2015). Molecular dynamic simulations reveal the structural determinants of Fatty Acid binding to oxy-myoglobin. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0128496"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"25133","DOI":"10.1074\/jbc.M116.754978","article-title":"Novel Molecular Interactions of Acylcarnitines and Fatty Acids with Myoglobin","volume":"291","author":"Chintapalli","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/0006-291X(77)90333-3","article-title":"Fatty acid binding to cytoplasmic proteins of myocardium and red and white skeletal muscle in the rat. A possible new role for myoglobin","volume":"74","author":"Gloster","year":"1977","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1515\/bchm3.1994.375.6.387","article-title":"Fatty acid binding of myoglobin depends on its oxygenation","volume":"375","author":"Gotz","year":"1994","journal-title":"Biol. Chem. Hoppe-Seyler"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1007\/s11745-017-4272-z","article-title":"Differential Interaction of Myoglobin with Select Fatty Acids of Carbon Chain Lengths C8 to C16","volume":"52","author":"Jue","year":"2017","journal-title":"Lipids"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1007\/s13105-017-0559-z","article-title":"Effect of fatty acid interaction on myoglobin oxygen affinity and triglyceride metabolism","volume":"73","author":"Jue","year":"2016","journal-title":"J. Physiol. Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"3643","DOI":"10.1016\/j.febslet.2008.09.047","article-title":"Interaction of fatty acid with myoglobin","volume":"582","author":"Sriram","year":"2008","journal-title":"FEBS Lett."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1152\/japplphysiol.00973.2013","article-title":"Changing the paradigm for myoglobin: A novel link between lipids and myoglobin","volume":"117","author":"Schlater","year":"2014","journal-title":"J. Appl. Physiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0309-1740(85)90051-8","article-title":"Metmyoglobin and inorganic metals as pro-oxidants in raw and cooked muscle systems","volume":"15","author":"Tichivangana","year":"1985","journal-title":"Meat Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/0003-9861(90)90427-Z","article-title":"Ferrylmyoglobin-catalyzed linoleic acid peroxidation","volume":"281","author":"Galaris","year":"1990","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0309-1740(97)00014-4","article-title":"Lipid oxidation induced by oxymyoglobin and metmyoglobin with involvement of H(2)O(2) and superoxide anion","volume":"46","author":"Chan","year":"1997","journal-title":"Meat Sci."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1021\/jf011169e","article-title":"Concentration effects in myoglobin-catalyzed peroxidation of linoleate","volume":"50","author":"Baron","year":"2002","journal-title":"J. Agric. Food Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1006\/bbrc.2000.2349","article-title":"Enhanced lipid oxidation by oxidatively modified myoglobin: Role of protein-bound heme","volume":"269","author":"Vuletich","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"3887","DOI":"10.1021\/jf011394w","article-title":"Myoglobin-induced lipid oxidation. A review","volume":"50","author":"Baron","year":"2002","journal-title":"J. Agric. Food Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"E47","DOI":"10.1152\/ajpendo.00662.2020","article-title":"On the potential role of globins in brown adipose tissue: A novel conceptual model and studies in myoglobin knockout mice","volume":"321","author":"Blackburn","year":"2021","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1161\/CIRCRESAHA.107.152488","article-title":"Nitrite reductase function of deoxymyoglobin: Oxygen sensor and regulator of cardiac energetics and function","volume":"100","author":"Rassaf","year":"2007","journal-title":"Circ. Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1152\/japplphysiol.00789.2012","article-title":"Interaction between myoglobin and mitochondria in rat skeletal muscle","volume":"114","author":"Yamada","year":"2013","journal-title":"J. Appl. Physiol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1021\/bi00866a027","article-title":"The interaction of myoglobin with mitochondrial structural protein","volume":"5","author":"Edwards","year":"1966","journal-title":"Biochemistry"},{"key":"ref_47","first-page":"1211","article-title":"Myoglobin and mitochondria: Oxymyoglobin interacts with mitochondrial membrane during deoxygenation","volume":"74","author":"Postnikova","year":"2009","journal-title":"Biochemistry"},{"key":"ref_48","first-page":"280","article-title":"Fluorescence studies on the interaction of myoglobin with mitochondria","volume":"77","author":"Postnikova","year":"2012","journal-title":"Biochemistry"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1002\/bmb.2005.494033032470","article-title":"Allosteric modulation of monomeric proteins","volume":"33","author":"Ascenzi","year":"2005","journal-title":"Biochem. Mol. Biol. Educ."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"16999","DOI":"10.1074\/jbc.271.29.16999","article-title":"Functional modulation by lactate of myoglobin. A monomeric allosteric hemoprotein","volume":"271","author":"Giardina","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"14859","DOI":"10.1021\/ja036166s","article-title":"On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?","volume":"125","author":"Turnbull","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"ref_52","first-page":"10","article-title":"Studies on pH-Controlled Transition of Myoglobin Capsules from Hollow to Multilayered Structures","volume":"33","author":"Kamatchi","year":"2015","journal-title":"J. Adsorpt. Sci. Technol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/0039-9140(94)80110-X","article-title":"Removal of dissolved oxygen from water: A comparison of four common techniques","volume":"41","author":"Butler","year":"1994","journal-title":"Talanta"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/0022-2836(80)90262-4","article-title":"Structure and refinement of oxymyoglobin at 1.6 A resolution","volume":"142","author":"Phillips","year":"1980","journal-title":"J. Mol. Biol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"6035","DOI":"10.1073\/pnas.76.12.6035","article-title":"Carbon monoxide binding to iron porphyrins","volume":"76","author":"Collman","year":"1979","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"5128","DOI":"10.1021\/bi00183a017","article-title":"Conformational relaxation and ligand binding in myoglobin","volume":"33","author":"Ansari","year":"1994","journal-title":"Biochemistry"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1016\/S0162-0134(00)80291-3","article-title":"Oxidation of nitrogen oxides by bound dioxygen in hemoproteins","volume":"14","author":"Doyle","year":"1981","journal-title":"J. Inorg. Biochem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/336265a0","article-title":"The role of the distal histidine in myoglobin and haemoglobin","volume":"336","author":"Olson","year":"1988","journal-title":"Nature"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1080\/15216540701230495","article-title":"Ligand pathways in myoglobin: A review of Trp cavity mutations","volume":"59","author":"Olson","year":"2007","journal-title":"IUBMB Life"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"11909","DOI":"10.1021\/bi970719s","article-title":"Ligand migration in sperm whale myoglobin","volume":"36","author":"Scott","year":"1997","journal-title":"Biochemistry"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"5177","DOI":"10.1074\/jbc.M008282200","article-title":"Mapping the pathways for O2 entry into and exit from myoglobin","volume":"276","author":"Scott","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1006\/jmbi.1993.1491","article-title":"Investigations of ligand association and dissociation rates in the \u201copen\u201d and \u201cclosed\u201d states of myoglobin","volume":"233","author":"Tian","year":"1993","journal-title":"J. Mol. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"762","DOI":"10.1006\/jmbi.1996.0123","article-title":"Crystal structures of CO-, deoxy- and met-myoglobins at various pH values","volume":"256","author":"Yang","year":"1996","journal-title":"J. Mol. Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1038\/1731236a0","article-title":"Solubility of oxygen in water","volume":"173","author":"Tuesdale","year":"1954","journal-title":"Nature"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility","volume":"30","author":"Morris","year":"2009","journal-title":"J. Comput. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1021\/ct100578z","article-title":"PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pKa Predictions","volume":"7","author":"Olsson","year":"2011","journal-title":"J. Chem. Theory Comput."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"E63","DOI":"10.1152\/ajpendo.00624.2020","article-title":"Metabolic physiology and skeletal muscle phenotypes in male and female myoglobin knockout mice","volume":"321","author":"Olfert","year":"2021","journal-title":"Am. J. Physiology. Endocrinol. Metab."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/9\/4747\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T23:01:01Z","timestamp":1760137261000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/23\/9\/4747"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,4,26]]},"references-count":67,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2022,5]]}},"alternative-id":["ijms23094747"],"URL":"https:\/\/doi.org\/10.3390\/ijms23094747","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,4,26]]}}}