Methods for nitrogenase-like dark operative protochlorophyllide oxidoreductase.
Methods for nitrogenase-like dark operative protochlorophyllide oxidoreductase.
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固氮酶样暗操作原叶绿素内酯氧化还原酶的方法
DOI:
10.1007/978-1-61779-194-9_9
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发表时间:
2011
影响因子:
--
通讯作者:
Bröcker
中科院分区:
文献类型:
--
作者:
Bröcker
Nitrogenase-like dark operative protochlorophyllide oxidoreductase (DPOR) is involved in the biosynthesis of chlorophylls and bacteriochlorophylls in gymnosperms, ferns, algae, and photosynthetic bacteria. During protochlorophyllide (Pchlide) reduction, the homodimeric subunit ChlL2of DPOR transfers electrons on the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)2. Although DPOR shares significant amino acid sequence homology to the nitrogenase system, only the initial catalytic steps of DPOR resemble nitrogenase catalysis. Investigation of the cyanobacterial DPOR fromProchlorococcus marinusindicated that subcomplex ChlL2is functioning as an ATP-dependent switch protein, triggering the transient interaction of ChlL2and (ChlN/ChlB)2. This dynamic subunit interplay is responsible for the transfer of a single electron from the [4Fe–4S] cluster of ChlL2onto a second [4Fe–4S] cluster located on (ChlN/ChlB)2. However, the second part of DPOR catalysis is unrelated to nitrogenase catalysis, since no molybdenum-containing cofactor or a P-cluster equivalent is employed. Instead, two consecutive electron transfer steps are mediated via the [4Fe–4S] cluster of (ChlN/ChlB)2, resulting in the reduction of the conjugated ring system of the substrate molecule Pchlide (Figs. 5.1aand5.2).
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影响因子:
4.8
作者:
Broecker, Markus J.;Waetzlich, Denise;Jahn, Dieter
通讯作者:
Jahn, Dieter
影响因子:
4.8
作者:
Broecker, Markus J.;Waetzlich, Denise;Jahn, Dieter
通讯作者:
Jahn, Dieter
影响因子:
4.8
作者:
Broecker, Markus J.;Virus, Simone;Moser, Juergen
通讯作者:
Moser, Juergen
影响因子:
2.1
作者:
J. Walther;M. Bröcker;Denise Wätzlich;M. Nimtz;M. Rohde;D. Jahn;J. Moser
通讯作者:
J. Moser