Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenase

Nitrogenase is a complicated enzyme that actives the ATP-dependent reduction of dinitrogen (N2) to ammonia (NH3). The aim of this manuscript is to review the nitrogenase evolution with considering nitrogenase, structure of nitrogenase, action mechanism of nitrogenase and oxygen sensitive mechanism...

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Main Authors: Wenli SUN, Mohamad Hesam SHAHRAJABIAN
Format: Article
Language:English
Published: AcademicPres 2024-02-01
Series:Notulae Botanicae Horti Agrobotanici Cluj-Napoca
Subjects:
Online Access:https://www.notulaebotanicae.ro/index.php/nbha/article/view/13157
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author Wenli SUN
Mohamad Hesam SHAHRAJABIAN
author_facet Wenli SUN
Mohamad Hesam SHAHRAJABIAN
author_sort Wenli SUN
collection DOAJ
description Nitrogenase is a complicated enzyme that actives the ATP-dependent reduction of dinitrogen (N2) to ammonia (NH3). The aim of this manuscript is to review the nitrogenase evolution with considering nitrogenase, structure of nitrogenase, action mechanism of nitrogenase and oxygen sensitive mechanism of nitrogenase. The searches focused on publications from 1980 to February 2023, using PubMed, Google Scholar, Science Direct, and Scopus databases. In the term of evolution, the nitrogen cycle has experienced highly changes; at the beginning of life and suggested the exact anoxic scenario, the comparatively sufficient ammonium was possibly used in an assimilation/mineralization cycle by protocellular organisms. The main nif gene products which are active in nitrogen fixation are nifH, nifD, nifK, nifT, nifY/nafY, nifE, nifN, nifX, nifU, nifS, nifV, nifW, nifZ, nifM, nifF, nifL, nifA, nifB, fdxN, nifQ, and nifJ. The main vnf gene products which are active in nitrogen fixation are vnfA, vnfE, vnfN, vnfX, vnfH, vnfFd, vnfD, vnfG, vnfK, and vnfY. Oxygen can be either detrimental or beneficial for diazotrophs in organisms suitable for an aerobic catabolism, and it supports the production of a substrate for nitrogenase (ATP), but it can also impede the activity and suppress the synthesis of this enzyme. 
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spelling doaj.art-2326c9fe28fd41528180a07fef9d9eb12024-04-01T18:50:06ZengAcademicPresNotulae Botanicae Horti Agrobotanici Cluj-Napoca0255-965X1842-43092024-02-0152110.15835/nbha52113157Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenaseWenli SUN0Mohamad Hesam SHAHRAJABIAN1National Key Laboratory of Agricultural Microbiology, Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, BeijingNational Key Laboratory of Agricultural Microbiology, Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing Nitrogenase is a complicated enzyme that actives the ATP-dependent reduction of dinitrogen (N2) to ammonia (NH3). The aim of this manuscript is to review the nitrogenase evolution with considering nitrogenase, structure of nitrogenase, action mechanism of nitrogenase and oxygen sensitive mechanism of nitrogenase. The searches focused on publications from 1980 to February 2023, using PubMed, Google Scholar, Science Direct, and Scopus databases. In the term of evolution, the nitrogen cycle has experienced highly changes; at the beginning of life and suggested the exact anoxic scenario, the comparatively sufficient ammonium was possibly used in an assimilation/mineralization cycle by protocellular organisms. The main nif gene products which are active in nitrogen fixation are nifH, nifD, nifK, nifT, nifY/nafY, nifE, nifN, nifX, nifU, nifS, nifV, nifW, nifZ, nifM, nifF, nifL, nifA, nifB, fdxN, nifQ, and nifJ. The main vnf gene products which are active in nitrogen fixation are vnfA, vnfE, vnfN, vnfX, vnfH, vnfFd, vnfD, vnfG, vnfK, and vnfY. Oxygen can be either detrimental or beneficial for diazotrophs in organisms suitable for an aerobic catabolism, and it supports the production of a substrate for nitrogenase (ATP), but it can also impede the activity and suppress the synthesis of this enzyme.  https://www.notulaebotanicae.ro/index.php/nbha/article/view/13157biological nitrogen fixationnitrogenasenitrogenase evolutionoxygenstructure of nitrogenase
spellingShingle Wenli SUN
Mohamad Hesam SHAHRAJABIAN
Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenase
Notulae Botanicae Horti Agrobotanici Cluj-Napoca
biological nitrogen fixation
nitrogenase
nitrogenase evolution
oxygen
structure of nitrogenase
title Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenase
title_full Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenase
title_fullStr Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenase
title_full_unstemmed Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenase
title_short Survey on nitrogenase evolution by considering the importance of nitrogenase, its structure, and mechanism of nitrogenase
title_sort survey on nitrogenase evolution by considering the importance of nitrogenase its structure and mechanism of nitrogenase
topic biological nitrogen fixation
nitrogenase
nitrogenase evolution
oxygen
structure of nitrogenase
url https://www.notulaebotanicae.ro/index.php/nbha/article/view/13157
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