NirJ, a radical SAM family member of the d1 heme biogenesis cluster

被引：22

作者：

Brindley, Amanda A. ^{[1
]}

Zajicek, Richard ^{[2
]}

Warren, Martin J. ^{[1
]}

Ferguson, Stuart J. ^{[2
]}

Rigby, Stephen E. J. ^{[3
]}

机构：

[1] Univ Kent, Dept Biosci, Prot Sci Grp, Canterbury CT2 7NJ, Kent, England

[2] Univ Oxford, Dept Biochem, Oxford OX1 3QU, England

[3] Univ Manchester, Manchester Interdisciplinary Bioctr, Fac Life Sci, Manchester M1 7DN, Lancs, England

来源：

FEBS LETTERS | 2010年 / 584卷 / 11期

基金：

英国生物技术与生命科学研究理事会;

关键词：

Biosynthesis; Tetrapyrrole; NirJ; Radical SAM; Iron-sulfur centre; Heme d(1); ADENOSYL-L-METHIONINE; S-ADENOSYLMETHIONINE; CRYSTAL-STRUCTURE; NITRITE REDUCTASE; LYSINE 2,3-AMINOMUTASE; BIOTIN SYNTHASE; GENE-CLUSTER; BIOSYNTHESIS; SUPERFAMILY; ENZYME;

D O I：

10.1016/j.febslet.2010.04.053

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：

NirJ is involved in the transformation of precorrin-2 into heme d(1), although its precise role in the process has not been established. The purified protein was found to contain a 4Fe-4S centre, in line with the prediction that it belongs to the radical SAM class of enzymes. This was further confirmed by binding of S-adenosyl-L-methionine (SAM) to dithionite-reduced NirJ, which resulted in a decrease in the signal intensity and in a shift to higher field of the [4Fe-4S](1+) EPR signal. Significantly, though, this approach also led to the appearance of a small but reproducible organic radical signal that was associated with about 2% of the NirJ molecules and was affected by the incorporation of SAM deuterated at the 5' adenosyl group. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：2461 / 2466

页数：6

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