Sobolev V, Edelman M
Department of Plant Genetics, Weizmann Institute of Science, Rehovot, Israel.
Proteins. 1995 Mar;21(3):214-25. doi: 10.1002/prot.340210304.
Functional identity and significant similarities in cofactors and sequence exist between the L and M reaction center proteins of the photosynthetic bacteria and the D1 and D2 photosystem-II reaction center proteins of cyanobacteria, algae, and plants. A model of the quinone (QB) binding site of the D1 protein is presented based upon the resolved structure of the QB binding pocket of the L subunit, and introducing novel quantitative notions of complementarity and contact surface between atoms. This model, built without using traditional methods of molecular mechanics and restricted to residues in direct contact with QB, accounts for the experimentally derived functional state of mutants of the D1 protein in the region of QB. It predicts the binding of both the classical and phenol-type PSII herbicides and rationalizes the relative levels of tolerance of mutant phenotypes.
光合细菌的L和M反应中心蛋白与蓝细菌、藻类和植物的D1和D2光系统II反应中心蛋白之间在辅因子和序列上存在功能一致性和显著相似性。基于L亚基的醌（QB）结合口袋的解析结构，并引入原子间互补性和接触表面的新定量概念，提出了D1蛋白的醌（QB）结合位点模型。该模型在构建时未使用传统的分子力学方法，且仅限于与QB直接接触的残基，解释了D1蛋白在QB区域突变体的实验推导功能状态。它预测了经典型和酚类PSII除草剂的结合，并合理化了突变体表型的相对耐受水平。
