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Volumn 68, Issue 5, 2004, Pages 1156-1159

Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome P450nor

Author keywords

Cytochrome P450nor; NADH binding; Nitric oxide reductase; Salt bridge network

Indexed keywords

ARGININE; ASPARTIC ACID; CYTOCHROME P450; GLUTAMIC ACID; HEME; NICOTINAMIDE ADENINE DINUCLEOTIDE; NITRIC OXIDE REDUCTASE (P450); NITRIC-OXIDE REDUCTASE (P450); OXIDOREDUCTASE;

EID: 4143088801     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.68.1156     Document Type: Article
Times cited : (8)

References (12)
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  • 5
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    • Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide (NO): Implication for its NO reduction mechanism
    • Shiro, Y., Fujii, M., Iizuka, T., Adachi, S., Tsukamoto, K., Nakahara, K., and Shoun, H., Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide (NO): Implication for its NO reduction mechanism. J. Biol. Chem., 270, 1617-1623 (1995).
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  • 7
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    • A positively charged cluster formed in the hemedistal pocket of cytochrome P450nor is essential for interaction with NADH
    • Kudo, T., Takaya, N., Park, S.-Y., Shiro, Y., and Shoun, H., A positively charged cluster formed in the hemedistal pocket of cytochrome P450nor is essential for interaction with NADH. J. Biol. Chem., 276, 5020-5026 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 5020-5026
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  • 8
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    • The B′ helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH
    • Zhang, L., Kudo, T., Takaya, N., and Shoun, H., The B′ helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH. J. Biol. Chem., 277, 33842-33847 (2002).
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  • 9
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    • Proton delivery in NO reduction by fungal nitric-oxide reductase: Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes
    • Shimizu, H., Obayashi, E., Gomi, Y., Arakawa, H., Park, S.-Y., Nakamura, H., Adachi, S., Shoun, H., and Shiro, Y., Proton delivery in NO reduction by fungal nitric-oxide reductase: Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes. J. Biol. Chem., 275, 4816-4826 (2000).
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  • 10
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    • Site-directed mutagenesis of the conserved threonine (Thr243) of the distal helix of fungal cytochrome P450nor
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    • D88A mutant of cytochrome P450nor provides kinetic evidence for direct complex formation with electron donor NADH
    • in press
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.