Reversible and irreversible hemichrome generation by the oxygenation of nitrosylmyoglobin

被引：22

作者：

Arnold, EV ^{[1
]}

Bohle, DS ^{[1
]}

Jordan, PA ^{[1
]}

机构：

[1] Univ Wyoming, Dept Chem, Laramie, WY 82071 USA

来源：

BIOCHEMISTRY | 1999年 / 38卷 / 15期

关键词：

D O I：

10.1021/bi982729e

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The repeated oxygenation/reduction/nitrosylation of nitrosylmyoglobin produces low-spin ferric heme hemichromes which have been characterized by electron spin resonance spectroscopy. The predominant myoglobin hemichrome is a chemically reversible dihistidyl complex identified by the g values 1.53, 2.21, and 2.97, Also present is a low-spin ferric hydroxide derivative which is represented by the g values 1.83, 2.18, and 2.59, The formation of these species goes undetected by UV-vis spectroscopy, but the oxygenation of myoglobin to metmyoglobin is correlated with complete conversion of nitric oxide to nitrate which is released following a clear induction period. These results are interpreted in terms of the intermediates generated during the MbNO oxygenation reaction.

引用

页码：4750 / 4756

页数：7

共 48 条

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