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Metabolism of Molybdenum

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Metallomics and the Cell

Part of the book series: Metal Ions in Life Sciences ((MILS,volume 12))

Abstract

The transition element molybdenum is of essential importance for (nearly) all biological systems. It needs to be complexed by a special cofactor in order to gain catalytic activity. With the exception of bacterial Mo-nitrogenase, where Mo is a constituent of the FeMo-cofactor, Mo is bound to a pterin, thus forming the molybdenum cofactor Moco, which in different versions is the active compound at the catalytic site of all other Mo-containing enzymes. In eukaryotes, the most prominent Mo enzymes are nitrate reductase, sulfite oxidase, xanthine dehydrogenase, aldehyde oxidase, and the mitochondrial amidoxime reductase. The biosynthesis of Moco involves the complex interaction of six proteins and is a process of four steps, which also requires iron, ATP, and copper. After its synthesis, Moco is distributed to the apoproteins of Mo enzymes by Moco-carrier/binding proteins. A deficiency in the biosynthesis of Moco has lethal consequences for the respective organisms. In humans, Moco deficiency is a severe inherited inborn error in metabolism resulting in severe neurodegeneration in newborns and causing early childhood death. Eubacteria possess different versions of the pteridin cofactor as reflected by a large number of enzymes such as nitrate reductase, formate dehydrogenase, and dimethyl sulfoxide reductase, while in archaea a tungsten atom replaced molybdenum as catalytic metal in the active center.

Please cite as: Met. Ions Life Sci. 12 (2013) 503–528

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Abbreviations

ABA3:

Moco sulfurase in plants

ABC:

ATP-binding cassette

AMP:

adenosine 5'-monophosphate

AO:

aldehyde oxidase

ATP:

adenosine 5'-triphosphate

CIA:

cytosolic iron-sulfur cluster assembly

CMP:

cytosine 5'-monophosphate

cPMP:

cyclic pyranopterin monophosphate

DMSO:

dimethylsulfoxide

ER:

endoplasmic reticulum

FAD:

flavin adenine dinucleotide

FeMoco:

iron-molybdenum cofactor

GTP:

guanosine 5'-triphosphate

HMCS:

Moco sulfurase in humans

ISC:

iron-sulfur cluster

mARC:

mitochondral amidoxime reducing component

MCD:

molybdopterin-cytosine dinucleotide cofactor

MCP:

Moco carrier protein

MGD:

molybdopterin-guanine dinucleotide

MoBP:

molybdenum cofactor binding protein

Moco:

molybdenum cofactor

MOCS:

molybdenum cofactor synthesis

MPT:

molybdopterin

NAD(P)H:

nicotinamide adenine dinucleotide (phosphate) reduced

NR:

nitrate reductase

RLD:

rhodanese-like domain

ROS:

reactive oxygen species

SAM:

S-adenosyl methionine

SO:

sulfite oxidase

Wco:

tungsten pterin-type cofactor

XDH:

xanthine dehydrogenase

XO:

xanthine oxidase

XOR:

xanthine oxidoreductase

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Acknowledgments

R.R.M. thanks the many people who worked with him over the years on molybdenum. In particular I am grateful to Florian Bittner, Robert Hänsch, and Tobias Kruse for many critical discussions and to Tobias Kruse for help with the figures. The research was consistenly supported by the Deutsche Forschungsgemeinschaft which is gratefully acknowledged.

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Authors and Affiliations

  1. Institute of Plant Biology, Braunschweig University of Technology, Humboldt Street 1, D-38106, Braunschweig, Germany

    Ralf R. Mendel

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  1. Ralf R. Mendel
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Correspondence to Ralf R. Mendel .

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  1. Centro Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, 50019, Firenze, Italy

    Lucia Banci

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Mendel, R.R. (2013). Metabolism of Molybdenum. In: Banci, L. (eds) Metallomics and the Cell. Metal Ions in Life Sciences, vol 12. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5561-1_15

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