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http://purl.uniprot.org/citations/10611283http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10611283http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10611283http://www.w3.org/2000/01/rdf-schema#comment"Cytochrome b-type NAD(P)H oxidoreductases are involved in many physiological processes, including iron uptake in yeast, the respiratory burst, and perhaps oxygen sensing in mammals. We have identified a cytosolic cytochrome b-type NAD(P)H oxidoreductase in mammals, a flavohemoprotein (b5+b5R) containing cytochrome b5 (b5) and b5 reductase (b5R) domains. A genetic approach, using BLAST searches against DBEST for FAD-, NAD(P)H-binding sequences followed by reverse transcription-PCR, was used to clone the complete cDNA sequence of human b5+b5R from the hepatoma cell line Hep 3B. Compared with the classical single-domain b5 and b5R proteins localized on endoplasmic reticulum membrane, b5+b5R also has binding motifs for heme, FAD, and NAD(P)H prosthetic groups but no membrane anchor. The human b5+b5R transcript was expressed at similar levels in all tissues and cell lines that were tested. The two functional domains b5* and b5R* are linked by an approximately 100-aa-long hinge bearing no sequence homology to any known proteins. When human b5+b5R was expressed as c-myc adduct in COS-7 cells, confocal microscopy revealed a cytosolic localization at the perinuclear space. The recombinant b5+b5R protein can be reduced by NAD(P)H, generating spectrum typical of reduced cytochrome b with alpha, beta, and Soret peaks at 557, 527, and 425 nm, respectively. Human b5+b5R flavohemoprotein is a NAD(P)H oxidoreductase, demonstrated by superoxide production in the presence of air and excess NAD(P)H and by cytochrome c reduction in vitro. The properties of this protein make it a plausible candidate oxygen sensor."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.26.14742"xsd:string
http://purl.uniprot.org/citations/10611283http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.26.14742"xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Huang S."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Huang S."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Zhu H."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Zhu H."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Qiu H."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Qiu H."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Bunn H.F."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Bunn H.F."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Yoon H.-W."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/author"Yoon H.-W."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/pages"14742-14747"xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/pages"14742-14747"xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/title"Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously expressed in human cells."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/title"Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously expressed in human cells."xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10611283http://purl.uniprot.org/core/volume"96"xsd:string