八聚体硫代硫酸盐还原酶是一种具有新型血红素连接方式的呼吸酶。
Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation.
作者信息
Mowat Christopher G, Rothery Emma, Miles Caroline S, McIver Lisa, Doherty Mary K, Drewette Katy, Taylor Paul, Walkinshaw Malcolm D, Chapman Stephen K, Reid Graeme A
机构信息
Institute of Cell and Molecular Biology, School of Biological Sciences, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK.
出版信息
Nat Struct Mol Biol. 2004 Oct;11(10):1023-4. doi: 10.1038/nsmb827. Epub 2004 Sep 7.
We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.
我们从奥奈达希瓦氏菌中分离出一种可溶性细胞色素，它含有八个共价连接的血红素基团，并确定了其晶体结构。其中一个血红素尽管通过典型的CXXCH基序连接，但铁原子却通过赖氨酸残基的ε-氨基进行了新颖的配位。这个血红素很可能是连四硫酸盐还原反应的活性位点，该反应由这种酶高效催化。
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