The fixation of atmospheric dinitrogen to ammonia by industrial technologies (such as the Haber Bosch process) has revolutionized humankind. In contrast to industrial technologies, a single enzyme is known for its ability to reduce or "fix" dinitrogen: nitrogenase. Nitrogenase is a complex oxidoreductase enzymatic system that includes a catalytic protein (where dinitrogen is reduced) and an electron-transferring reductase protein (termed the Fe protein) that delivers the electrons necessary for dinitrogen fixation. The catalytic protein most commonly contains a FeMo cofactor (called the MoFe protein), but it can also contain a VFe or FeFe cofactor. Besides their ability to fix dinitrogen to ammonia, these nitrogenases can also reduce substrates such as carbon dioxide to formate. Interestingly, the VFE nitrogenase can also form carbon-carbon bonds. The vast majority of research surrounding nitrogenase employs the Fe protein to transfer electrons, which is also associated with the rate-limiting step of nitrogenase catalysis and also requires the hydrolysis of adenosine triphosphate. Thus, there is significant interest in artificially transferring electrons to the catalytic nitrogenase proteins. In this Account, we review nitrogenase electrocatalysis whereby electrons are delivered to nitrogenase from electrodes. We first describe the use of an electron mediator (cobaltocene) to transfer electrons from electrodes to the MoFe protein. The reduction of protons to molecular hydrogen was realized, in addition to azide and nitrite reduction to ammonia. Bypassing the rate-limiting step within the Fe protein, we also describe how this approach was used to interrogate the rate-limiting step of the MoFe protein: metal-hydride protonolysis at the FeMo-co. This Account next reviews the use of cobaltocene to mediate electron transfer to the VFe protein, where the reduction of carbon dioxide and the formation of carbon-carbon bonds (yielding the formation of ethene and propene) was realized. This approach also found success in mediating electron transfer to the FeFe catalytic protein, which exhibited improved carbon dioxide reduction in comparison to the MoFe protein. In the final example of mediated electron transfer to the catalytic protein, this Account also reviews recent work where the coupling of infrared spectroscopy with electrochemistry enabled the potential-dependent binding of carbon monoxide to the FeMo-co to be studied. As an alternative to mediated electron transfer, recent work that has sought to transfer electrons to the catalytic proteins in the absence of electron mediators (by direct electron transfer) is also reviewed. This approach has subsequently enabled a thermodynamic landscape to be proposed for the cofactors of the catalytic proteins. Finally, this Account also describes nitrogenase electrocatalysis whereby electrons are first transferred from an electrode to the Fe protein, before being transferred to the MoFe protein alongside the hydrolysis of adenosine triphosphate. In this way, increased quantities of ammonia can be electrocatalytically produced from dinitrogen fixation. We discuss how this has led to the further upgrade of electrocatalytically produced ammonia, in combination with additional enzymes (diaphorase, alanine dehydrogenase, and transaminase), to selective production of chiral amine intermediates for pharmaceuticals. This Account concludes by discussing current and future research challenges in the field of electrocatalytic nitrogen fixation by nitrogenase.

Ross D. Milton

Shelley D. Minteer

Accounts of Chemical Research

ACCOUNTS OF CHEMICAL RESEARCH 提供简短、简洁和批判性的文章，提供化学和生物化学所有领域的基础研究和应用的易于阅读的概述。此外，ACCOUNTS OF CHEMICAL RESEARCH 还出版了专门针对具有不寻常活动和意义的单一问题的特刊。访问 ACCOUNTS SPECIAL ISSUES 页面，查看所有特殊问题的列表、描述和 TOC。从 2008 年开始，ACCOUNTS OF CHEMICAL RESEARCH 将其传统的文章摘要替换为文章“CONSPECTUS”。这些新条目概述了研究，使读者可以更仔细地了解文章的内容和意义。通过对文章内容的更详细描述，CONSPECTUS 提高了文章在搜索引擎中的可发现性和研究的曝光率。

Accounts of Chemical Research publishes concise, clear, and critical articles that provide accessible overviews of fundamental research and applications across all areas of chemistry and biochemistry. Additionally, Accounts of Chemical Research publishes special issues focused on single topics of unusual activity and significance. You can visit the Accounts of Chemical Research Special Issues page to view a list of all special issues, their descriptions, and tables of contents. Since 2008, Accounts of Chemical Research has replaced traditional article abstracts with 'CONSPECTUS.' These new entries summarize the research, allowing readers to gain a deeper understanding of the content and significance of the articles. By providing a more detailed description of the article content, CONSPECTUS enhances the discoverability of articles in search engines and increases the visibility of the research.

《Accounts of Chemical Research》提供简短、清晰且具有批判性的文章，涵盖化学和生物化学各个领域的基础研究和应用，旨在为读者提供易于理解的概述。此外，《Accounts of Chemical Research》还出版专门针对具有特殊活动和重要性的单一主题的特刊。您可以访问《Accounts of Chemical Research》特刊页面，查看所有特刊的列表、描述和目录。从2008年开始，《Accounts of Chemical Research》将传统的文章摘要替换为“CONSPECTUS”，这些新条目概述了研究内容，使读者能够更深入地理解文章的内容和意义。通过对文章内容的详细描述，CONSPECTUS提高了文章在搜索引擎中的可发现性和研究的曝光率。

Category	Quartile
化学	1
化学, 化学综合	1

Nitrogenase Bioelectrochemistry for Synthesis Applications

ivySCI AI Smartly Parses PDF, Answers Researchers' Questions, and Helps You Understand Papers in Seconds

Journal Info

Category	Quartile
CHEMISTRY, MULTIDISCIPLINARY	1