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对来自集胞藻6803(Synechocystis sp. PCC 6803)的一种还原NAD(P)的镍氢化酶的操纵子进行序列分析,为该酶与NAD(P)H脱氢酶(复合体I)的直接偶联提供了更多证据。

Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P)H-dehydrogenase (complex I).

作者信息

Appel J, Schulz R

机构信息

Philipps-Universität, Marburg, Germany.

出版信息

Biochim Biophys Acta. 1996 Dec 5;1298(2):141-7. doi: 10.1016/s0167-4838(96)00176-8.

Abstract

The sequence of a NAD(P)-reducing hydrogenase operon of Synechocystis sp. PCC 6803 containing genes for a small and a large hydrogenase subunit and six additional ORFs was determined. Until now only 11 of the 14 polypeptides of the NADH-dehydrogenase of E. coli were found in Synechocystis. By sequence homologies we suggest that the missing subunits of the peripheral part of the dehydrogenase, containing most of the FeS-clusters, are encoded by three ORFs of this operon. This hypothesis is discussed in relation to the NAD(P)-reducing hydrogenase of Synechocystis.

摘要

测定了集胞藻PCC 6803中一个NAD(P)还原氢化酶操纵子的序列,该操纵子包含一个小的和一个大的氢化酶亚基基因以及另外六个开放阅读框。到目前为止,在集胞藻中仅发现了大肠杆菌NADH脱氢酶14种多肽中的11种。通过序列同源性,我们认为该操纵子的三个开放阅读框编码了脱氢酶外围部分缺失的亚基,这些亚基包含大部分FeS簇。结合集胞藻的NAD(P)还原氢化酶对这一假设进行了讨论。

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