Molybdenum Trafficking for Nitrogen Fixation

Hernández, José Ángel; George, Simon J.; Rubio, Luis M.

doi:10.1021/bi901217p

Cited by 64 publications

(49 citation statements)

References 116 publications

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“…Panel e shows a simplified FeMo-co biosynthetic pathway illustrating the two putative pathways for molybdenum incorporation into the Mo-nitrogenase cofactor. Reproduced from Hernandez et al (2009). With kind permission of © Biochemistry dissociation steps between the Fe protein and the MoFe protein, and the sequential, inter-protein transfer of electrons from the (4Fe-4S) cluster of the Fe protein, through the P-cluster, to the FeMoco of the MoFe protein, where substrate is reduced (Hu and Ribbe 2011).…”

Section: Biochemical Aspectsmentioning

confidence: 99%

Nitrogen Fixation, a Molybdenum-Requiring Process

Presta

Fondi

Emiliani

et al. 2015

SpringerBriefs in Molecular Science

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Nitrogen fixation is the most important input of biologically available nitrogen in Earth's ecosystems and is a metabolic ability possessed only by some Prokaryotes. To date four classes of nitrogenase enzymes have been characterized. Three nitrogenases are homologous enzymes with similar protein subunit composition and metal cofactor structure; these are the Mo-nitrogenase, V-nitrogenase, and Fe-only nitrogenase. How these three systems evolved and which of them first appeared on Earth is still under debate. The best studied system is the Fe-Mo-co based although several comparative analyses have been performed in past years.In Chap. 4 only the class of pterin-based (Mo-co) molybdenum enzymes was discussed. However, there is an enzyme that uses a different form of Mo-cofactor (Fig. 5.1), the aforementioned nitrogenase, which catalyses the conversion of atmospheric nitrogen into ammonia, a process known as biological nitrogen fixation. Before entering nitrogenase's biochemical structure and the relative metabolic pathway, an overview of nitrogen fixation process will be provided.

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Section: Biochemical Aspectsmentioning

confidence: 99%

Nitrogen Fixation, a Molybdenum-Requiring Process

Presta

Fondi

Emiliani

et al. 2015

SpringerBriefs in Molecular Science

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“…Mo is also required in nitrogenase, the key enzyme of nitrogen fixation (Hernandez et al, 2009, Schwarz et al, 2009). In the absence of fixed forms of N, diazotrophic (N 2 -fixing) organisms synthesize nitrogenase at levels up to 10% of total cell protein, which places a high demand for the corresponding metal ion cofactors (Dingler et al, 1988).…”

Section: Microbial Adaptation and Acclimation To Metal Ion Limitmentioning

confidence: 99%

“…Similarly, Rhodobacter capsulatus expresses an alternative Fe-only nitrogenase (containing a cofactor designated FeFe-co) in response to Mo limitation. In general, these alternative nitrogenases are not as efficient as is the MoFe enzyme (Hernandez et al, 2009). …”

Section: Microbial Adaptation and Acclimation To Metal Ion Limitmentioning

confidence: 99%

Elemental Economy

Merchant

Helmann

2012

Advances in Microbial Physiology

182

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“…Molybdenum (Mo) is an essential trace element for archea, bacteria, and eukaryotes (e.g., Williams and Fraústo da Silva, 2002; Zhang and Gladyshev, 2008; Hernandez et al, 2009). More than 60 metalloenzymes and proteins have been identified containing Mo (Lippard et al, 1994; Hille, 1996; Kisker et al, 1997; Stiefel, 1997, 1998; Kroneck and Abt, 2002; Boll et al, 2005; NC-IUB, 2012; ExPASy, 2012), including nitrogenase and nitrate reductase, which tie the element to the nitrogen cycle (e.g., Kroneck and Abt, 2002).…”

Section: Introductionmentioning

confidence: 99%

Redox chemistry of molybdenum in natural waters and its involvement in biological evolution

Wang

2012

Front. Microbio.

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The transition element molybdenum (Mo) possesses diverse valances (+II to +VI), and is involved in forming cofactors in more than 60 enzymes in biology. Redox switching of the element in these enzymes catalyzes a series of metabolic reactions in both prokaryotes and eukaryotes, and the element therefore plays a fundamental role in the global carbon, nitrogen, and sulfur cycling. In the present oxygenated waters, oxidized Mo(VI) predominates thermodynamically, whilst reduced Mo species are mainly confined within specific niches including cytoplasm. Only recently has the reduced Mo(V) been separated from Mo(VI) in sulfidic mats and even in some reducing waters. Given the presence of reduced Mo(V) in contemporary anaerobic habitats, it seems that reduced Mo species were present in the ancient reducing ocean (probably under both ferruginous and sulfidic conditions), prompting the involvement of Mo in enzymes including nitrogenase and nitrate reductase. During the global transition to oxic conditions, reduced Mo species were constrained to specific anaerobic habitats, and efficient uptake systems of oxidized Mo(VI) became a selective advantage for current prokaryotic and eukaryotic cells. Some prokaryotes are still able to directly utilize reduced Mo if any exists in ambient environments. In total, this mini-review describes the redox chemistry and biogeochemistry of Mo over the Earth’s history.

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Molybdenum Trafficking for Nitrogen Fixation

Cited by 64 publications

References 116 publications

Nitrogen Fixation, a Molybdenum-Requiring Process

Nitrogen Fixation, a Molybdenum-Requiring Process

Elemental Economy

Redox chemistry of molybdenum in natural waters and its involvement in biological evolution

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