{"title":"MECHANISTIC FEATURES OF THE MO-CONTAINING NITROGENASE.","authors":"J. Christiansen, D. Dean, L. Seefeldt","doi":"10.1146/ANNUREV.ARPLANT.52.1.269","DOIUrl":null,"url":null,"abstract":"Nitrogenase is the complex metalloenzyme responsible for biological dinitrogen reduction. This reaction represents the single largest contributor to the reductive portion of the global nitrogen cycle. Recent developments in understanding the mechanism of the Mo-based nitrogenase are reviewed. Topics include how nucleotide binding and hydrolysis are coupled to electron transfer and substrate reduction, how electrons are accumulated and transferred within the MoFe-protein, and how substrates bind and are reduced at the active site metal cluster.","PeriodicalId":80493,"journal":{"name":"Annual review of plant physiology and plant molecular biology","volume":"57 1","pages":"269-295"},"PeriodicalIF":0.0000,"publicationDate":"2001-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/ANNUREV.ARPLANT.52.1.269","citationCount":"115","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Annual review of plant physiology and plant molecular biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1146/ANNUREV.ARPLANT.52.1.269","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 115
Abstract
Nitrogenase is the complex metalloenzyme responsible for biological dinitrogen reduction. This reaction represents the single largest contributor to the reductive portion of the global nitrogen cycle. Recent developments in understanding the mechanism of the Mo-based nitrogenase are reviewed. Topics include how nucleotide binding and hydrolysis are coupled to electron transfer and substrate reduction, how electrons are accumulated and transferred within the MoFe-protein, and how substrates bind and are reduced at the active site metal cluster.