Identification of the ligand trans to thiolate in cytochrome P‐450 LM2 by chemical modification

FEBS Letters

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.

【 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