Structure of the primary donor of Rhodopseudomonas sphaeroides: difference resonance Raman spectroscopy of reaction centers
Structure of the primary donor of Rhodopseudomonas sphaeroides: difference resonance Raman spectroscopy of reaction centers
复制标题
球形红假单胞菌主要供体的结构：反应中心的差异共振拉曼光谱
DOI：
10.1021/bi00357a001
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发表时间：
1986
期刊：
影响因子：
2.9
通讯作者：
M. Lutz
中科院分区：
文献类型：
--
作者：
B. Robert;M. Lutz
Service de Biophysique，Département de Biologie，Centre d 'Etudes Nucléaires de Saclay，91191 Gif-sur-Yvette Cedex，France接收于1986年1月7日;修订的Mandarin pt接收于1986年2月28日摘要：通过使用差分方法，从野生型球形红球藻的反应中心获得了处于基态和中性状态的主要供体的共振拉曼光谱。三种不同的方法产生了基本相同的差异光谱，从两个不等价的细菌叶绿素a分子。这些光谱允许的镁原子和酮和乙酰羰基的主要捐助者细菌叶绿素的分子相互作用状态进行描述。根据这些数据，建立了Rps主要供体的分子模型。sphaeroides野生型。该模型不涉及两个细菌叶绿素之间的相互结合的相互作用，在中性，基态，通过其镁原子和乙酰基carbonyls.The细菌光合作用的第一步，涉及创建一个供体-受体离子对从捕获的能量入射光子，发生在专门的膜结合的色素蛋白质复合物命名为反应中心（RC）。1这些蛋白复合物已经从几种细菌中分离出高纯度但功能性的状态（Gingras，
Service de Biophysique, Département de Biologie, Centre d’Etudes Nucléaires de Saclay, 91191 Gif-sur-Yvette Cedex, France Received January 7, 1986; Revised Manuscript Received February 28, 1986 abstract: ResonanceRaman spectra of the primary donor in its ground, neutral state were obtained from reaction centers of Rhodopseudomonas sphaeroides, wild type, by using difference methods. Three distinct methods yielded essentially identical difference spectra, arising from two unequivalent bacteriochlorophyll a molecules. These spectra permitted the molecular interaction states of the magnesium atoms and of the keto and acetyl carbonyls of the primary donor bacteriochlorophylls to be described. From these data, a molecular model of the primary donor of Rps. sphaeroides, wild type, is proposed. This model involves no mutual binding interactions between the two bacteriochlorophylls, in the neutral, groundstate, through their magnesium atoms and their acetyl carbonyls.The first steps of bacterial photosynthesis, involving the creation of a donor-acceptor ion pair from trapped energy of incoming photons, occur in specialized membrane-bound pigment-protein complexes named reaction centers (RC). 1 These proteic complexes have been isolatedin highly pure yet functional states from several species of bacteria (Gingras,