Procaryotic complex I (NDH-1), an overview.
Procaryotic complex I (NDH-1), an overview.
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DOI:
10.1016/s0005-2728(98)00023-1
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发表时间:
1998-05
期刊:
影响因子:
--
通讯作者:
Takao Yagi;Takahiro Yano;Salvatore Di Bernardo;A. Matsuno‐Yagi
中科院分区:
文献类型:
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作者:
Takao Yagi;Takahiro Yano;Salvatore Di Bernardo;A. Matsuno‐Yagi
NADH-ubiquinone UQ oxidoreductase. Therefore, in this article, we designate the NADH dehydrogenase in the respiratory chain as NADH-Q oxidoreductase. In addition, the bacterial proton-translocating NADH-Q oxidoreductase is designated NADH dehy-Ž. drogenase I NDH-1 because Kaback and his colw x leagues 5–8 initially designated this enzyme com-Ž. plex as NADH dehydrogenase I NDH-1 to distin-Ž. guish it from NADH dehydrogenase II NDH-2, which lacks an energy coupling site. Therefore, we use this terminology after the pioneering work of Kaback and his colleagues on the bacterial NADH-Q oxidoreductases. In this article, NDH-1 and complex I refer to bacterial and mitochondrial proton-translocating enzyme complexes, respectively. In the previous chapter, the articles have reviewed present knowledge of structure and function of mitochondrial complex I. This chapter is concerned with its bacterial counterparts, NDH-1. Following this artiwx wx cle, Friedrich 9 and Dupuis et al. 10 describe recent progress in studies of the NDH-1 in Escherichia coli and Rhodobacter capsulatus, respectively. Therefore, we attempted to provide general and wide information about the NDH-1 and also cover present knowledge of other bacterial NDH-1.