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Pterin-Containing Microbial Molybdenum Enzymes

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Microbial Metabolism of Metals and Metalloids

Part of the book series: Advances in Environmental Microbiology ((AEM,volume 10))

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Abstract

In this chapter, several facets of microbial molybdenum enzymes are discussed. First, the sources and uptake of molybdenum into cells, as well as cofactor synthesis, are reviewed. Genes involved in cofactor synthesis are mentioned along with whether or not they have a well-defined function. The biogeochemical importance as well as evolutionary origin of the cofactor and relationship to phylogenetic classification are examined. Representative structures of microbial molybdenum enzymes from the three main families (xanthine oxidase, sulfite oxidase, and dimethyl sulfoxide (DMSO) reductase) are also included. The functions of these enzyme families have been well accepted. This chapter also highlights select general mechanisms that are still under discussion, such as oxygen atom transfer (OAT) and hydroxylation, as well as catalytic cycles of specific enzymes. The chapter also includes sections on amino acids near the metal center and other amino acids that influence either substrate specificity or mechanistic properties.

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Acknowledgments

We thank our past and present coworkers and collaborators who have inspired us with stimulating discussions. We are grateful for financial support from the National Institutes of Health and National Science Foundation for support of our work on microbial molybdenum enzymes.

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  1. Department of Chemistry & Chemical Biology, Indiana University - Purdue University Indianapolis, Indianapolis, IN, USA

    Mikayla C. Metzger & Partha Basu

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    Christon J. Hurst

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Metzger, M.C., Basu, P. (2022). Pterin-Containing Microbial Molybdenum Enzymes. In: Hurst, C.J. (eds) Microbial Metabolism of Metals and Metalloids. Advances in Environmental Microbiology, vol 10. Springer, Cham. https://doi.org/10.1007/978-3-030-97185-4_13

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