The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria

Leimkühler, Silke; Wuebbens, Margot M.; Rajagopalan, K.V.

doi:10.1016/j.ccr.2010.12.003

Cited by 123 publications

(157 citation statements)

References 148 publications

(228 reference statements)

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“…Analysis of Moco-deficient mutants in a given organism ranging from bacteria to plants and humans resulted in the identification of several gene loci involved in Moco biosynthesis (2,11). Along with the conserved structure of Moco, these findings provided a basis to propose an evolutionary old multistep biosynthesis pathway (20).…”

Section: Molybdenum Cofactor Biosynthesismentioning

confidence: 99%

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The Molybdenum Cofactor

Mendel

2013

Journal of Biological Chemistry

244

181

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The transition element molybdenum needs to be complexed by a special cofactor to gain catalytic activity. Molybdenum is bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants, is the active compound at the catalytic site of all molybdenum-containing enzymes in nature, except bacterial molybdenum nitrogenase. The biosynthesis of Moco involves the complex interaction of six proteins and is a process of four steps, which also require iron, ATP, and copper. After its synthesis, Moco is distributed, involving Mocobinding proteins. A deficiency in the biosynthesis of Moco has lethal consequences for the respective organisms.The transition element molybdenum is an essential micronutrient for microorganisms, plants, and animals (1). Surprisingly, molybdenum itself is catalytically inactive in biological systems until it is complexed by a special scaffold (2). One type of scaffold is the ubiquitous pterin-based molybdenum cofactor (Moco), 2 which, in different variants, forms part of the active centers of all molybdenum enzymes in living organisms, except one. This exception is bacterial nitrogenase, which harbors the other type of cofactor, namely the Fe-S cluster-based FeMo cofactor, which is found only once in nature (for details, compare the minireview of Hu and Ribbe (62) in this thematic series). Molybdenum belongs to the group of trace elements, i.e. the organism needs it only in minute amounts; however, unavailability of molybdenum is lethal for the organism. Molybdenum is very abundant in the oceans in the form of the molybdate anion (3). In soils, the molybdate anion is the only form of molybdenum that is available for bacteria, plants, and fungi. More than 50 enzymes are known to be molybdenumdependent. The vast majority of them are found in bacteria, whereas only seven have been identified in eukaryotes (4, 5). It is somewhat surprising that not all organisms need molybdenum. The commonly used eukaryotic model organism yeast plays no role in molybdenum research, as Saccharomyces cerevisiae does not contain either molybdenum enzymes or the Moco biosynthesis pathway. Also Schizosaccharomyces pombe does not use molybdenum, whereas Pichia pastoris needs molybdenum. Genome-wide database analyses revealed a significant number of bacteria and unicellular eukaryotes that do not need molybdenum, whereas all multicellular eukaryotes are dependent on molybdenum (6). In addition, mainly anaerobic archaea and some bacteria are molybdenum-independent, but they require tungsten for their growth (7). In the periodic table of elements, tungsten lies directly below molybdenum and features chemical properties similar to molybdenum.Molybdenum metabolism is tightly connected to Fe-S cluster synthesis in that some of the molybdenum enzymes and Moco biosynthesis itself depend on Fe-S enzymes and on a mitochondrial transporter that is known to be crucial for the maturation of cytosolic Fe-S proteins. Moreover, Moco biosynthesis recruits mechanisms previously known from Fe-S cluster synthe...

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Section: Molybdenum Cofactor Biosynthesismentioning

confidence: 99%

“…In this minireview, I will focus on higher organisms (eukaryotes). Bacterial Moco variants were recently reviewed in detail (11).…”

Section: What Is the Molybdenum Cofactor?mentioning

confidence: 99%

The Molybdenum Cofactor

Mendel

2013

Journal of Biological Chemistry

244

181

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“…The biosynthesis of the molybdenum cofactor (Moco) is a highly conserved and complex pathway (60,111). For instance, in E. coli, nine proteins with known function are directly involved in Moco biosynthesis (35,112).…”

Section: Guanosine 5′-triphosphate (Gtp)mentioning

confidence: 99%

“…Although the highly-labile and complex MobisPGD cofactor is an essential component for DMSO reductase activity, understanding its insertion in the maturation pathway poses as a challenge to understanding CISM folding. Currently, it is postulated that MoeB and MoaA are involved in the final cofactor hand-off during CISM maturation (60)(61)(62)(63).…”

Section: Stage 5: Molybdenum Cofactor (Moco) Insertionmentioning

confidence: 99%

Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

Cherak

Turner

2017

Biomolecular Concepts

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Protein folding and assembly into macromolecule complexes within the living cell are complex processes requiring intimate coordination. The biogenesis of complex iron sulfur molybdoenzymes (CISM) requires use of a system specific chaperone -a redox enzyme maturation protein (REMP) -to help mediate final folding and assembly. The CISM dimethyl sulfoxide (DMSO) reductase is a bacterial oxidoreductase that utilizes DMSO as a final electron acceptor for anaerobic respiration. The REMP DmsD strongly interacts with DMSO reductase to facilitate folding, cofactor-insertion, subunit assembly and targeting of the multi-subunit enzyme prior to membrane translocation and final assembly and maturation into a bioenergetic catalytic unit. In this article, we discuss the biogenesis of DMSO reductase as an example of the participant network for bacterial CISM maturation pathways.

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“…Microorganisms having capability to reduce heavy metals such as chromium, molybdenum mercury into less toxic forms were documented. Molybdenum (Mo) is essential to organisms as it is a cofactor to many important enzymes such as nitrogenase, sulfite oxidase, aldehyde oxidase and xanthine oxidoreductase (Daniels et al 2008;Leimkühler et al 2011). Molybdenum is not generally toxic to human.…”

Section: Introductionmentioning

confidence: 99%

ISOLATION AND CHARACTERIZATION OF A MOLYBDENUM-REDUCING AND PHENOLIC- AND CATECHOL-DEGRADING Enterobacter sp. STRAIN SAW-2

Sabullah

Rahman²,

Ahmad³

et al. 2017

BIOTROPIA

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Molybdenum is an emerging pollutant worldwide. The objective of this study is to isolate molybdenum-reducing bacterium with the ability to grow on phenolic compounds (phenol and catechol). The screening process was carried out on a microplate. The bacterium reduced molybdenum in the form of sodium molybdate to molybdenum blue (Mo-blue). The bacterium required a narrow pH range for optimal reduction of molybdenum, i.e. between pH 6.3 and o 6.8, with temperature between 34 and 37 C. Molybdate reduction to Mo-blue was best supported by glucose as the carbon source. However, both phenol and catechol could not support molybdate reduction. Other requirements for molybdate reduction included sodium molybdate concentrations between 15 and 30 mM, and phosphate concentration of 5.0 mM. The bacterium exhibited a Mo-blue absorption spectrum with a shoulder at 700 nm and a maximum peak near the infrared region at 865 nm. The Mo-reducing bacterium was partially identified as Enterobacter sp. strain Saw-2. The capability of this bacterium to grow on toxic phenolic compounds and to detoxify molybdenum made it a significant agent for bioremediation.

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The history of the discovery of the molybdenum cofactor and novel aspects of its biosynthesis in bacteria

Cited by 123 publications

References 148 publications

The Molybdenum Cofactor

The Molybdenum Cofactor

Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

ISOLATION AND CHARACTERIZATION OF A MOLYBDENUM-REDUCING AND PHENOLIC- AND CATECHOL-DEGRADING Enterobacter sp. STRAIN SAW-2

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