期刊论文详细信息
FEBS Letters
Identification of the ligand trans to thiolate in cytochrome P‐450 LM2 by chemical modification
Ruckpaul, K.1  Dettmer, R.2  Jänig, G.-R.1  Usanov, S.A.3 
[1] Department of Biocatalysis, Central Institute of Molecular Biology, GDR Academy of Sciences, 1115 Berlin-Buch, GDR;Department of Analytic and Biotechnology, Central Institute of Molecular Biology, GDR Academy of Sciences, 1115 Berlin-Buch, GDR;Institute of Bioorganic Chemistry, Belorussian Academy of Sciences, Minsk 220600, USSR
关键词: Cytochrome P-450;    Active center;    Sixth ligand;    Tyrosine;    Chemical modification;   
DOI  :  10.1016/0014-5793(83)80416-5
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

About 3 tyrosine residues of cytochrome P-450 LM2 are accessible to chemical modification with tetranitromethane. Nitration of two tyrosines inactivates the enzyme to about 20%. The partial formation of a hyper-porphyrin spectrum originating from the pK shift by nitration and formation of a tyrosinate is prevented by modification in the presence of the inhibitor metyrapone. These findings support the assumption of a tyrosine residue as sixth ligand of the heme iron in cytochrome P-450 LM2.

【 授权许可】

Unknown   

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