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嗜热古菌嗜热甲烷热菌中氢化酶和多铁氧化还原蛋白结构的保守性

Conservation of hydrogenase and polyferredoxin structures in the hyperthermophilic archaebacterium Methanothermus fervidus.

作者信息

Steigerwald V J, Beckler G S, Reeve J N

机构信息

Department of Microbiology, Ohio State University, Columbus 43210.

出版信息

J Bacteriol. 1990 Aug;172(8):4715-8. doi: 10.1128/jb.172.8.4715-4718.1990.

DOI:10.1128/jb.172.8.4715-4718.1990
PMID:2115877
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC213312/
Abstract

A 3.3-kilobase-pair region of the Methanothermus fervidus genome encoding part of the small subunit and all of the large subunit of the methyl viologen-reducing hydrogenase and a polyferredoxin was cloned and sequenced. The sequence of this hyperthermophilic hydrogenase conforms to the consensus sequence established for procaryotic [NiFe] hydrogenases. Although the M. fervidus polyferredoxin is the same size as the Methanobacterium thermoautotrophicum ferredoxin, containing six tandemly arranged bacterial ferredoxinlike domains, these two proteins are predicted to be only 64% identical in their primary sequences.

摘要

克隆并测序了嗜热栖热菌基因组中一个3.3千碱基对的区域，该区域编码甲基紫精还原氢化酶小亚基的一部分和大亚基的全部以及一种聚铁氧化还原蛋白。这种嗜热氢化酶的序列符合原核生物[NiFe]氢化酶所确立的共有序列。虽然嗜热栖热菌聚铁氧化还原蛋白与嗜热自养甲烷杆菌铁氧化还原蛋白大小相同，都含有六个串联排列的细菌铁氧化还原蛋白样结构域，但预计这两种蛋白质的一级序列只有64%相同。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd7c/213312/c2d080df76da/jbacter00122-0595-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd7c/213312/c2d080df76da/jbacter00122-0595-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cd7c/213312/c2d080df76da/jbacter00122-0595-a.jpg

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