{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,16]],"date-time":"2023-10-16T21:56:09Z","timestamp":1697493369106},"reference-count":47,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2005,8,1]],"date-time":"2005-08-01T00:00:00Z","timestamp":1122854400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,1]],"date-time":"2020-09-01T00:00:00Z","timestamp":1598918400000},"content-version":"vor","delay-in-days":5510,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Lipid Research"],"published-print":{"date-parts":[[2005,8]]},"DOI":"10.1194\/jlr.m500034-jlr200","type":"journal-article","created":{"date-parts":[[2005,6,2]],"date-time":"2005-06-02T00:35:19Z","timestamp":1117672519000},"page":"1660-1667","source":"Crossref","is-referenced-by-count":15,"title":["Studies on the specificity of unprocessed and mature forms of phytanoyl-CoA 2-hydroxylase and mutation of the iron binding ligands"],"prefix":"10.1016","volume":"46","author":[{"given":"Timothy","family":"Searls","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Danica","family":"Butler","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Winnie","family":"Chien","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mridul","family":"Mukherji","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Matthew D.","family":"Lloyd","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christopher J.","family":"Schofield","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1194\/jlr.M500034-JLR200_bib1","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1023\/A:1005476631419","article-title":"The metabolism of phytanic acid and pristanic acid in man: a review","volume":"21","author":"Verhoeven","year":"1998","journal-title":"J. Inherit. Metab. Dis."},{"key":"10.1194\/jlr.M500034-JLR200_bib2","series-title":"The Metabolic and Molecular Bases of Inherited Disease","first-page":"3303","article-title":"Refsum disease","author":"Wanders","year":"2001"},{"key":"10.1194\/jlr.M500034-JLR200_bib3","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1093\/jnen\/60.11.1021","article-title":"Refsum disease, peroxisomes and phytanic acid oxidation: a review","volume":"60","author":"Wanders","year":"2001","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1194\/jlr.M500034-JLR200_bib4","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/S0022-2275(20)34204-8","article-title":"Phytanic acid and pristanic acid are oxidised by sequential peroxisomal and mitochondrial reactions in cultured fibroblasts","volume":"39","author":"Verhoeven","year":"1998","journal-title":"J. Lipid Res."},{"key":"10.1194\/jlr.M500034-JLR200_bib5","series-title":"Handbook of Ataxia Disorders","first-page":"235","article-title":"Heredopathia atactica polyneuritiformis: Refsum's disease","author":"Gibberd","year":"2000"},{"key":"10.1194\/jlr.M500034-JLR200_bib6","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1046\/j.0022-3042.2002.00766.x","article-title":"Refsum's disease: a peroxisomal disorder affecting phytanic acid metabolism \u03b1-oxidation","volume":"80","author":"Wierzbicki","year":"2002","journal-title":"J. Neurochem."},{"key":"10.1194\/jlr.M500034-JLR200_bib7","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1056\/NEJM199707103370215","article-title":"Phytanoyl-coenzyme A hydroxylase deficiency\u2014the enzyme defect in Refsum's disease","volume":"337","author":"Jansen","year":"1997","journal-title":"N. Engl. J. Med."},{"key":"10.1194\/jlr.M500034-JLR200_bib8","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/ng1097-185","article-title":"Identification of PAHX, a Refsum disease gene","volume":"17","author":"Mihalik","year":"1997","journal-title":"Nat. Genet."},{"key":"10.1194\/jlr.M500034-JLR200_bib9","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1093\/hmg\/9.8.1195","article-title":"Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease","volume":"9","author":"Jansen","year":"2000","journal-title":"Hum. Mol. Genet."},{"key":"10.1194\/jlr.M500034-JLR200_bib10","first-page":"649","article-title":"Identification of genetic heterogeneity in Refsum's disease","volume":"8","author":"Wierzbicki","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1194\/jlr.M500034-JLR200_bib11","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S1074-5521(02)00139-4","article-title":"Utilization of sterol carrier protein-2 by phytanoyl-CoA 2 hydroxylase in the peroxisomal \u03b1-oxidation of phytanic acid","volume":"9","author":"Mukherji","year":"2002","journal-title":"Chem. Biol."},{"key":"10.1194\/jlr.M500034-JLR200_bib12","doi-asserted-by":"crossref","first-page":"2349","DOI":"10.1194\/jlr.M300230-JLR200","article-title":"Further studies on the substrate spectrum of phytanoyl-CoA hydroxylase: implications for Refsum disease?","volume":"44","author":"Foulon","year":"2003","journal-title":"J. Lipid Res."},{"key":"10.1194\/jlr.M500034-JLR200_bib13","doi-asserted-by":"crossref","first-page":"7558","DOI":"10.1074\/jbc.M210385200","article-title":"Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau","volume":"278","author":"Lee","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib14","doi-asserted-by":"crossref","first-page":"1802","DOI":"10.1074\/jbc.C200644200","article-title":"Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1","volume":"278","author":"Elkins","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib15","doi-asserted-by":"crossref","first-page":"15351","DOI":"10.1073\/pnas.202614999","article-title":"Structure of factor-inhibiting hypoxia-inducible factor 1: an asparaginyl hydroxylase involved in the hypoxic response pathway","volume":"99","author":"Dann","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1194\/jlr.M500034-JLR200_bib16","doi-asserted-by":"crossref","first-page":"5185","DOI":"10.1021\/bi016014e","article-title":"X-ray crystal structure of Escherichia coli taurine\/\u03b1-ketoglutarate dioxygenase complexed to ferrous iron and substrates","volume":"41","author":"Elkins","year":"2002","journal-title":"Biochemistry."},{"key":"10.1194\/jlr.M500034-JLR200_bib17","doi-asserted-by":"crossref","first-page":"6625","DOI":"10.1046\/j.0014-2956.2001.02617.x","article-title":"Structure of proline 3-hydroxylase: evolution of the family of 2-oxoglutarate dependent oxygenases","volume":"268","author":"Clifton","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1194\/jlr.M500034-JLR200_bib18","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1038\/72398","article-title":"Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase","volume":"7","author":"Zhang","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1194\/jlr.M500034-JLR200_bib19","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1006\/jmbi.1999.2594","article-title":"Studies on the active site of deacetoxycephalosporin C synthase","volume":"287","author":"Lloyd","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1194\/jlr.M500034-JLR200_bib20","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/29575","article-title":"Structure of a cephalosporin synthase","volume":"394","author":"Valegard","year":"1998","journal-title":"Nature."},{"key":"10.1194\/jlr.M500034-JLR200_bib21","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/S0969-2126(01)00695-5","article-title":"Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana","volume":"10","author":"Wilmouth","year":"2002","journal-title":"Structure."},{"key":"10.1194\/jlr.M500034-JLR200_bib22","doi-asserted-by":"crossref","first-page":"1971","DOI":"10.1093\/hmg\/10.18.1971","article-title":"Structure-function analysis of phytanoyl-CoA 2-hydroxylase mutations causing Refsum's disease","volume":"10","author":"Mukherji","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"10.1194\/jlr.M500034-JLR200_bib23","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1039\/a902197c","article-title":"The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism","volume":"17","author":"Prescott","year":"2000","journal-title":"Nat. Prod. Rep."},{"key":"10.1194\/jlr.M500034-JLR200_bib24","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1039\/b101039p","article-title":"\u2018Chemical co-substrate rescue\u2019 of phytanoyl-CoA 2-hydroxylase mutants causing Refsum's disease","volume":"11","author":"Mukherji","year":"2001","journal-title":"Chem. Commun."},{"key":"10.1194\/jlr.M500034-JLR200_bib25","doi-asserted-by":"crossref","first-page":"2545","DOI":"10.1016\/S0960-894X(01)00494-2","article-title":"Studies on phytanoyl-CoA 2-hydroxylase and synthesis of phytanoyl-coenzyme A","volume":"11","author":"Kershaw","year":"2001","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1194\/jlr.M500034-JLR200_bib26","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/S0022-2275(20)32411-1","article-title":"Phytanoyl-CoA hydroxylase: recognition of 3-methyl-branched acyl-CoAs and requirement for GTP or ATP and Mg2+ in addition to its known hydroxylation cofactors","volume":"41","author":"Croes","year":"2000","journal-title":"J. Lipid Res."},{"key":"10.1194\/jlr.M500034-JLR200_bib27","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1194\/jlr.M500034-JLR200_bib28","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1111\/j.1432-1033.1995.545zz.x","article-title":"Phytanic acid \u03b1-oxidation in rat liver peroxisomes. Production of \u03b1-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors","volume":"232","author":"Mihalik","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"10.1194\/jlr.M500034-JLR200_bib29","doi-asserted-by":"crossref","first-page":"10157","DOI":"10.1074\/jbc.M211058200","article-title":"The selectivity and inhibition of AlkB","volume":"278","author":"Welford","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib30","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/S0162-0134(03)80525-1","article-title":"Mettalocenter characterization of AlkB, a mononuclear non-heme Fe(II) DNA repair enzyme","volume":"96","author":"Hausinger","year":"2003","journal-title":"J. Inorg. Biochem."},{"key":"10.1194\/jlr.M500034-JLR200_bib31","doi-asserted-by":"crossref","first-page":"26351","DOI":"10.1074\/jbc.C200273200","article-title":"Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family","volume":"277","author":"Hewitson","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib32","doi-asserted-by":"crossref","first-page":"2149","DOI":"10.1021\/ic00260a028","article-title":"Comparison of the stabilities of monomeric metal ion complexes formed with adenosine 5\u2032-triphosphates (ATP) and pyrimidine-nucleoside 5\u2032-triphosphates (CTP, UTP, TTP) and evaluation of the isomeric equilibria in the complexes of ATP and CTP","volume":"26","author":"Sigel","year":"1987","journal-title":"Inorg. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib33","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1007\/PL00000904","article-title":"Substrate selectivity studies on deacetoxycephalosporin C synthase using a direct spectrophotometric assay","volume":"58","author":"Dubus","year":"2001","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1194\/jlr.M500034-JLR200_bib34","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1006\/abio.1999.4203","article-title":"A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry","volume":"273","author":"Getz","year":"1999","journal-title":"Anal. Biochem."},{"key":"10.1194\/jlr.M500034-JLR200_bib35","doi-asserted-by":"crossref","first-page":"2648","DOI":"10.1021\/jo00008a014","article-title":"Selective reduction of disulphides by tris(2-carboxyenthyl)phosphine","volume":"56","author":"Burns","year":"1991","journal-title":"J. Org. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib36","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1006\/abio.1994.1290","article-title":"A procedure for quantitative determination of tris(2-carboxyethyl)phosphine, an odourless reducing agent more stable and effective than dithiothreitol","volume":"220","author":"Han","year":"1994","journal-title":"Anal. Biochem."},{"key":"10.1194\/jlr.M500034-JLR200_bib37","doi-asserted-by":"crossref","first-page":"9948","DOI":"10.1021\/bi9907532","article-title":"(S)-Mandelate dehydrogenase from Pseudomonas putida: mutations of the catalytic base histidine-274 and the chemical rescue of activity","volume":"38","author":"Lehoux","year":"1999","journal-title":"Biochemistry."},{"key":"10.1194\/jlr.M500034-JLR200_bib38","doi-asserted-by":"crossref","first-page":"7913","DOI":"10.1021\/bi00445a054","article-title":"Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant","volume":"28","author":"Tu","year":"1989","journal-title":"Biochemistry."},{"key":"10.1194\/jlr.M500034-JLR200_bib39","doi-asserted-by":"crossref","first-page":"17988","DOI":"10.1016\/S0021-9258(17)32407-9","article-title":"Comparison of intra- and intermolecular proton transfer in human carbonic anhydrase II","volume":"269","author":"Taoka","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib40","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/S0005-2728(00)00061-X","article-title":"Marcus rate theory applied to enzymatic proton transfer","volume":"1458","author":"Silverman","year":"2000","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1194\/jlr.M500034-JLR200_bib41","doi-asserted-by":"crossref","first-page":"12788","DOI":"10.1021\/bi9609331","article-title":"Rescue of the horseradish peroxidase His-170 to Ala mutant activity by imidazole: importance of proximal ligand tethering","volume":"35","author":"Newmyer","year":"1996","journal-title":"Biochemistry."},{"key":"10.1194\/jlr.M500034-JLR200_bib42","doi-asserted-by":"crossref","first-page":"14891","DOI":"10.1074\/jbc.271.25.14891","article-title":"Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles","volume":"271","author":"Newmyer","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib43","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1006\/bbrc.2000.3915","article-title":"Mutagenesis studies on the iron binding ligand of clavaminic acid synthase","volume":"279","author":"Doan","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1194\/jlr.M500034-JLR200_bib44","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/0076-6879(88)58067-9","article-title":"Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples","volume":"158","author":"Fish","year":"1988","journal-title":"Methods Enzymol."},{"key":"10.1194\/jlr.M500034-JLR200_bib45","doi-asserted-by":"crossref","first-page":"14332","DOI":"10.1021\/bi0480335","article-title":"Assignment of endogenous substrates to enzymes by global metabolite profiling","volume":"43","author":"Saghatelian","year":"2004","journal-title":"Biochemistry."},{"key":"10.1194\/jlr.M500034-JLR200_bib46","doi-asserted-by":"crossref","first-page":"48562","DOI":"10.1074\/jbc.M406649200","article-title":"The human FA2H gene encodes a fatty acid 2-hydroxylase","volume":"279","author":"Alderson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1194\/jlr.M500034-JLR200_bib47","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1038\/ng1097-190","article-title":"Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene","volume":"17","author":"Jansen","year":"1997","journal-title":"Nat. Genet."}],"container-title":["Journal of Lipid Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022227520329655?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022227520329655?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1194\/jlr.M500034-JLR200","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,20]],"date-time":"2021-11-20T17:03:01Z","timestamp":1637427781000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022227520329655"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,8]]},"references-count":47,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2005,8]]}},"alternative-id":["S0022227520329655"],"URL":"https:\/\/doi.org\/10.1194\/jlr.m500034-jlr200","relation":{},"ISSN":["0022-2275"],"issn-type":[{"value":"0022-2275","type":"print"}],"subject":[],"published":{"date-parts":[[2005,8]]}}}