STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER-SPHAEROIDES R-26 - PROTEIN COFACTOR (QUINONES AND FE-2+) INTERACTIONS .5.
STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER-SPHAEROIDES R-26 - PROTEIN COFACTOR (QUINONES AND FE-2+) INTERACTIONS .5.
复制标题
DOI：
10.1073/pnas.85.22.8487
复制
发表时间：
1988-11-01
影响因子：
11.1
通讯作者：
REES, DC
中科院分区：
文献类型：
--
作者：
ALLEN, JP;FEHER, G;REES, DC
用X-射线衍射法测定了球形红杆菌反应中心的三维结构，分辨率为2.8°，R值为24%。并与绿色红假单胞菌RCS的相互作用进行了比较。描述了对苯二酚起作用的QA和QB环境之间的结构差异(从QA-到QB的电子转移和QA-、QB-与主给电子体的电荷复合)。鉴定了可能参与QB质子化的蛋白质残基。提出了一种双还原QB与RC解离的途径。描述了QB与除草剂抗性突变体中发生变化的残基之间的相互作用。非血红素铁的环境与其他蛋白质中金属离子的环境进行了比较。
The three-dimensional structure of the reaction center (RC) from Rhodobacter sphaeroides has been determined by x-ray diffraction to a resolution of 2.8 .ANG. with an R value of 24%. The interactions of the protein with the primary quinone, QA, secondary quinone, QB, and the nonheme iron are described and compared to those of RCs from Rhodopseudomonas viridis. Structural differences between the QA and QB environments that contribute to the function of the quinones (the electron transfer from QA- to QB and the charge recombination of QA-, QB- with the primary donor) are delineated. The protein residues that may be involved in the protonation of QB are identified. A pathway for the doubly reduced QB to dissociate from the RC is proposed. The interactions between QB and the residues that have been changed in herbicide-resistant mutants are described. The environment of the nonheme iron is compared to the environments of metal ions in other proteins.