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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AcademicPres
2024-02-01
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Series: | Notulae Botanicae Horti Agrobotanici Cluj-Napoca |
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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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first_indexed | 2024-04-24T15:42:29Z |
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institution | Directory Open Access Journal |
issn | 0255-965X 1842-4309 |
language | English |
last_indexed | 2024-04-24T15:42:29Z |
publishDate | 2024-02-01 |
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series | Notulae Botanicae Horti Agrobotanici Cluj-Napoca |
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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