Melissa Chanderban Data-verified
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Researcher
unknown
Research Areas
Biography and Research Information
OverviewAI-generated summary
Melissa Chanderban's research focuses on the regulation of nitrogenase expression in archaea, specifically within the species *Methanosarcina acetivorans*. Her work investigates how environmental factors, such as the availability of molybdenum and fixed nitrogen, influence the production of different types of nitrogenases, including molybdenum, vanadium, and iron-only nitrogenases. Chanderban has explored the role of specific regulatory proteins, such as ModE, in controlling the expression of these alternative nitrogenases.
Her publications also address the function of hydrogenase in relation to nitrogen fixation in non-hydrogenotrophic methanogens. Chanderban collaborates with researchers at the University of Arkansas at Fayetteville, including Daniel J. Lessner and Thomas M. Deere, on studies related to these topics. Her scholarly output includes six publications with an h-index of 3, accumulating 28 citations.
Metrics
- h-index: 3
- Publications: 6
- Citations: 30
Selected Publications
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Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex (2025)
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<scp>ModE</scp> Regulates Alternative Nitrogenase Expression in the Methanogen <scp><i>Methanosarcina acetivorans</i></scp> (2025)
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Expression of V-nitrogenase and Fe-nitrogenase in <i>Methanosarcina acetivorans</i> is controlled by molybdenum, fixed nitrogen, and the expression of Mo-nitrogenase (2023)
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Methanosarcina acetivorans (2022)
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Vht hydrogenase is required for hydrogen cycling during nitrogen fixation by the non-hydrogenotrophic methanogen <i>Methanosarcina acetivorans</i> (2021)
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<i>Methanosarcina acetivorans</i> simultaneously produces molybdenum, vanadium, and iron-only nitrogenases in response to fixed nitrogen and molybdenum depletion (2021)
Collaboration Network
Top Collaborators
- Expression of V-nitrogenase and Fe-nitrogenase in <i>Methanosarcina acetivorans</i> is controlled by molybdenum, fixed nitrogen, and the expression of Mo-nitrogenase
- Methanosarcina acetivorans
- Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
- <i>Methanosarcina acetivorans</i> simultaneously produces molybdenum, vanadium, and iron-only nitrogenases in response to fixed nitrogen and molybdenum depletion
- Vht hydrogenase is required for hydrogen cycling during nitrogen fixation by the non-hydrogenotrophic methanogen <i>Methanosarcina acetivorans</i>
Showing 5 of 6 shared publications
- Expression of V-nitrogenase and Fe-nitrogenase in <i>Methanosarcina acetivorans</i> is controlled by molybdenum, fixed nitrogen, and the expression of Mo-nitrogenase
- <i>Methanosarcina acetivorans</i> simultaneously produces molybdenum, vanadium, and iron-only nitrogenases in response to fixed nitrogen and molybdenum depletion
- Vht hydrogenase is required for hydrogen cycling during nitrogen fixation by the non-hydrogenotrophic methanogen <i>Methanosarcina acetivorans</i>
- Methanosarcina acetivorans
- Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
- Vht hydrogenase is required for hydrogen cycling during nitrogen fixation by the non-hydrogenotrophic methanogen <i>Methanosarcina acetivorans</i>
- Expression of V-nitrogenase and Fe-nitrogenase in <i>Methanosarcina acetivorans</i> is controlled by molybdenum, fixed nitrogen, and the expression of Mo-nitrogenase
- <i>Methanosarcina acetivorans</i> simultaneously produces molybdenum, vanadium, and iron-only nitrogenases in response to fixed nitrogen and molybdenum depletion
- Vht hydrogenase is required for hydrogen cycling during nitrogen fixation by the non-hydrogenotrophic methanogen <i>Methanosarcina acetivorans</i>
- Methanosarcina acetivorans
- Methanosarcina acetivorans
- Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
- Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
- Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
- Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
- Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
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