换一批
换一批External loops at the ferredoxin-NADP(+) reductase protein-partner binding cavity contribute to substrates allocation.
第一作者：
Ana,Sánchez-Azqueta
第一单位：
Departamento de Bioquímica Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, Zaragoza, Spain; Institute of Biocomputation Physics of Complex Systems (BIFI)-Joint Unit BIFI-IQFR (CSIC), Universidad de Zaragoza, Zaragoza, Spain.
作者：
关键词
2′-P-AMP2′-P-AMP moiety of NADP(+)/H5-deazariboflavinCTCCatalytically competent interactionCharge-transfer complexETElectron and hydride transferFNRFNR in the anionic hydroquinone (fully reduced) stateFNR in the fully oxidized stateFNR in the partially reduced stateFNR(hq)FNR(ox)FNR(sq)FdFd(rd)Ferredoxin-NADP(+) reductaseHTIIsoalloxazine:nicotinamide interactionNMNPPiWTassociation and dissociation rate constants, respectively, for complex formationcharge-transfer complexdRfelectron transferelectron transfer rate constantferredoxinferredoxin in the reduced stateferredoxin-NADP(+) reductasehydride transferionic strengthk(1) and k(-1)k(2)k(HT)k(HT-1,) hydride transfer first-order rate constants for the forward and reverse reactions, respectivelyk(et)k(obs)nicotinamide nucleotide moiety of NADP(+)/Hobserved pseudo first-order rate constantpyrophosphatesecond-order rate constanwild-type
主题词
氨基酸序列(Amino Acid Sequence);鱼腥藻属(Anabaena);结合部位(Binding Sites);生物催化(Biocatalysis);辅酶类(Coenzymes);结晶学, X线(Crystallography, X-Ray);电子转运(Electron Transport);铁氧化还原蛋白NADP还原酶(Ferredoxin-NADP Reductase);铁氧化还原蛋白类(Ferredoxins);动力学(Kinetics);模型, 分子(Models, Molecular);分子序列数据(Molecular Sequence Data);突变蛋白质类(Mutant Proteins);蛋白质结合(Protein Binding);蛋白质结构, 二级(Protein Structure, Secondary);分光光度法, 紫外线(Spectrophotometry, Ultraviolet);构效关系(Structure-Activity Relationship);底物特异性(Substrate Specificity)
DOI
10.1016/j.bbabio.2013.11.016
PMID
24321506
发布时间
2016-11-26
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