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首页> 外文期刊>Biochemistry >Does Histidine 332 of the D1 Polypeptide Ligate the Manganese Cluster in Photosystem II? An Electron SpiN Echo Envelope Modulation Study
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Does Histidine 332 of the D1 Polypeptide Ligate the Manganese Cluster in Photosystem II? An Electron SpiN Echo Envelope Modulation Study

机译：D1多肽的组氨酸332是否会封闭光系统II中的锰簇？电子SpiN回波包络调制研究

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摘要

The tetranuclear manganese cluster in photosystem n is ligated by one or more histidine residues, s shown by an electron spin echo envelope modulation (ESEEM) study conducted with r5N]histidine- lbeled photosystem n particles isolated from the cyanobacterium Synechocystis sp. strain PCC 6803 rang, X.-S., Diner, B. A., Larsen, B. S., Gilchrist, M. L., Jr., Lorigan, G. A., and Britt, R. D. (1994) 'roc. Natl. Acad. Sci. U.S.A. 9] ,704-708]. One of these residues may be His332 of the Dl polypeptide. Ihotosystem n particles isolated from the Synechocystis mutant DI-H332E exhibit an altered S2 state rlultiline EPR signal that has more hyperfine lines and narrower splittings than the corresponding signal 11 wild-type psn particles [Debus, R. J., Campbell, K. A., Peloquin, J. M., Pham, D. P., and Britt, R. D. 2000) Biochemistry 39,470-478]. These DI-H332E psn particles are also unable to advance beyond n altered S2YZo state, and the quantum yield for forming the S2 state is very low, corresponding to an OOO-fold slowing of the rate of Mn oxidation by y zO. These observations are consistent with His332 ,eing close to the Mn cluster and modulating the redox properties of both the Mn cluster and tyrosine y z. '0 determine if DI-His332 ligates the Mn cluster, we have conducted an ESEEM study of DI-H332E 'sn particles. The histidyl nitrogen modulation observed near 5 MHz in ESEEM spectra of the S2 state rlultiline EPR signal of wild-type psn particles is substantially diminished in DI-H332E psn particles. 'his result is consistent with ligation of the Mn cluster by DI-His332. However, alternate explanations re possible. These are presented and discussed.
机译：光系统n中的四核锰簇与一个或多个组氨酸残基相连，这是通过对电子自旋回波包络调制（ESEEM）研究所进行的，该研究是使用从蓝藻拟蓝藻中分离的r5N]组氨酸光系统n粒子进行的。菌株PCC 6803 rang，X.-S.，Diner，B.A.，Larsen，B.S.，Gilchrist，M.L.，Jr.，Lorigan，G.A.和Britt，R.D.（1994）'roc。 Natl。学院科学[美国9]，704-708]。这些残基之一可以是D1多肽的His332。从集胞藻突变体DI-H332E分离出的Ihotosystem n粒子显示出比相应的信号11个野生型psn粒子[Debus，RJ，Campbell，KA，Peloquin，JM， Pham，DP和Britt，RD 2000），Biochemistry 39，470-478]。这些DI-H332E psn粒子也无法前进到超过n改变的S2YZo态，并且形成S2态的量子产率非常低，与y zO导致的Mn氧化速率减慢了OOO倍。这些观察结果与His332一致，即接近Mn团簇并调节Mn团簇和酪氨酸y z的氧化还原特性。 '0确定DI-His332是否连接Mn簇，我们已经对DI-H332E'sn颗粒进行了ESEEM研究。在DI-H332E psn颗粒中，在野生型psn颗粒的S2状态rlultiline EPR信号的ESEEM光谱中，在5 MHz附近观察到的组氨酸氮调制显着降低。他的结果与DI-His332连接锰簇相一致。但是，可以有其他解释。这些将被介绍和讨论。

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