首页    期刊浏览 2024年11月24日 星期日
登录注册

文章基本信息

  • 标题:Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle
  • 本地全文:下载
  • 作者:R V Hageman ; R H Burris
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1978
  • 卷号:75
  • 期号:6
  • 页码:2699-2702
  • DOI:10.1073/pnas.75.6.2699
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Nitrogenase and nitrogenase reductase dissociate after each electron is transferred between them, as shown by the occurrence of a lag phase approximately as long as the average turnover time of nitrogenase before hydrogen evolution occurs. Because nitrogenase was present in the reaction mixture in large excess over nitrogenase reductase, the electrons donated by nitrogenase reductase must have been distributed randomly over all of the nitrogenase present. This is accomplished by nitrogenase reductase molecules associating randomly with nitrogenase molecules for each cycle of electrons transferred. The fact that ATP is hydrolyzed without a lag indicates both that electron transfer occurs during the lag and the ATP hydrolysis is coupled to electron transfer from nitrogenase reductase to nitrogenase and not to substrate reduction. The observations support the suggestion that it now is desirable to alter nomenclature to designate the MoFe protein as nitrogenase and the Fe protein as nitrogenase reductase.
国家哲学社会科学文献中心版权所有