评论“钼氮酶还原 N 过程中金属辅因子的动态结构证据”。
Comment on "Structural evidence for a dynamic metallocofactor during N reduction by Mo-nitrogenase".
机构信息
Institute of Biological Chemistry, Washington State University, Pullman, WA 99164, USA.
Institute of Biochemistry, Albert-Ludwigs Universität, Freiburg, Germany.
出版信息
Science. 2021 Feb 12;371(6530). doi: 10.1126/science.abe5481.
Abstract
Kang (Reports, 19 June 2020, p. 1381) report a structure of the nitrogenase MoFe protein that is interpreted to indicate binding of N or an N-derived species to the active-site FeMo cofactor. Independent refinement of the structure and consideration of biochemical evidence do not support this claim.
摘要
康（Reports，2020 年 6 月 19 日，第 1381 页）报道了一种氮酶 MoFe 蛋白的结构，该结构被解释为表明 N 或 N 衍生物种与活性位点 FeMo 辅因子结合。对结构的独立细化和对生化证据的考虑并不支持这一说法。
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