Plastocyanin cytochrome f interaction.
Plastocyanin cytochrome f interaction.
复制标题
质体蓝素细胞色素 f 相互作用。
DOI：
10.1021/bi00446a011
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发表时间：
1989
期刊：
影响因子：
2.9
通讯作者：
Davis,DJ
中科院分区：
文献类型：
--
作者：
Morand,LZ;Frame,MK;Colvert,KK;Johnson,DA;Krogmann,DW;Davis,DJ
阿肯色州大学化学和生物化学系，费耶特维尔，阿肯色州72701，和普渡大学生物化学系，西拉斐特，印第安纳州47907，1989年3月13日接收; 1989年5月31日接收修订的Mandarin pt摘要：菠菜质体蓝素和芜菁细胞色素通过使用水溶性碳二亚胺共价连接，产生两种蛋白质的加合物。加合物中细胞色素/的氧化还原电位比游离细胞色素/的氧化还原电位移动了-20 mV，而加合物中质体蓝素的氧化还原电位与游离质体蓝素的氧化还原电位相同。溶剂扰动的研究表明，血红素暴露在加合物的程度是小于在游离细胞色素/，表明质体蓝素连接在这样一种方式，以掩埋暴露的血红素边缘。当加合物的共振拉曼光谱与游离的细胞色素相比时，也观察到微小的变化。加合物不能与光系统I相互作用或向光系统I提供电子。肽图和测序研究揭示了这两个蛋白质之间的两个连接位点。在连接的一个位点，质体蓝素的Asp-44共价连接到细胞色素l的Lys-187。这代表了第一次鉴定细胞色素/参与与质体蓝素相互作用的一个组。另一个连接位点涉及质体蓝素的Glu-59和/或Glu-60与细胞色素l上尚未鉴定的氨基基团。裸藻cytochromec-552也可以共价连接到芜菁细胞色素/，虽然效率低于菠菜质体蓝素。相反，多种蓝藻细胞色素c-553和蓝藻质体蓝素不能共价连接到芜菁细胞色素c-553上。光合电子传递链的细胞色素/（cyt f）1在两个光系统之间起作用，使用来自Rieske f的电子还原质体蓝素（PC），部分由NSF Grant DCB-8722411（DWK）、USDA Grant 87-CRCR 1 -2310和NIH Grant 2-S 07-RR 07101（DJD）支持，和DOD大学研究仪器资助N 00014 -85-G-0002（DAJ）。
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, Arkansas 72701, and Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907 Received March 13, 1989; Revised Manuscript Received May 31, 1989 abstract: Spinach plastocyanin and turnip cytochrome/have been covalently linked by using a water-soluble carbodiimide to yield an adduct of the two proteins. The redox potential of cytochrome/in the adduct was shifted by-20 mVrelative to that of free cytochrome/while the redox potential of plastocyanin in the adduct was the same as that of free plastocyanin. Solvent perturbation studies showed the degree of heme exposure in the adduct to be less than in free cytochrome/, indicating that plastocyanin was linked in such a way as to bury the exposed heme edge. Small changes were also observed when the resonance Raman spectrum of the adduct was compared to that of free cytochrome/. The adduct was incapable of interacting with or donating electrons to photosystem I. Peptide mapping and sequencing studies revealed two sites of linkage between thetwo proteins. In one site of linkage, Asp-44 of plastocyanin is covalently linked to Lys-187 of cytochrome/. This represents the first identification of a group on cytochrome/that is involved in the interaction with plastocyanin. The other site of linkage involves Glu-59 and/or Glu-60 of plastocyanin to as yet unidentified aminogroups on cytochrome/. Euglena cytochromec-552 could also be covalently linked to turnip cytochrome/, although with a lower efficiency than spinach plastocyanin. In contrast, a variety of cyanobacterial cytochrome c-553’s and a cyanobacterial plastocyanin couldnot be covalently linked to turnip cytochrome/.(cytochrome/(cyt f) 1 of the photosynthetic electrontransport chain functions between the two photosystems to reduce plastocyanin (PC) using electrons from the Rieske f Supported in part by NSF Grant DCB-8722411 (DWK), USDA Grant 87-CRCR1-2310 and NIH Grant2-S07-RR07101 (DJD), and DOD University Research Instrumentation Grant N00014-85-G-0002 (DAJ).