CHAPTER 1. Molybdenum and Tungsten-Containing Enzymes: An Overview

Maia, Luísa B.; Moura, Isabel; Moura, José J. G.

doi:10.1039/9781782623915-00001

Cited by 36 publications

(80 citation statements)

References 304 publications

(436 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…As for the tungsten-enzymes, due to their similarity with DMSO reductases, some authors group them together. However, other more accurate classifications (based on the metal/cofactor structure), as stated by Maia and co-workers, classify the tungsten-enzymes in a separate family from DMSO reductases [11]. In this review, the classification presented is the following: Xanthine oxidases, sulfite oxidases, tungsten-enzymes, and DMSO reductases (Table 1).…”

Section: Families Of Enzymes Containing Molybdenum or Tungstenmentioning

confidence: 97%

“…The family of sulfite oxidases is present in three domains of life and its main feature is the coordination of the MoCo by pyranopterin where Mo is covalently bound by a cysteine of the polypeptide chain of the enzyme (Table 1). They have also two oxo groups and the sulfurs of the cis-dithiolene group [11]. In the sulfite oxidases family, there are not only reductases, but also oxidases.…”

Section: Families Of Enzymes Containing Molybdenum or Tungstenmentioning

confidence: 99%

“…On the one hand, vanadium is present alternatively to the FeMoCo in some nitrogenases, as part of the iron-vanadium cofactor (FeVCo) [10]. On the other hand, tungsten is present as cofactor in tungsten enzymes, sharing a lot of resemblances with the MoCo of DMSO reductases [11].…”

Section: Introductionmentioning

confidence: 99%

“…Tungstate (WO 4 −2 ) is the biologically available form of W and is present in lower concentrations than MoO 2 −4 in oceans. Under euxinic conditions such as those characterizing hydrothermal vents (similar conditions to the ancient Earth), Mo forms MoS 2 , which is insoluble, whilst W forms soluble salts (WS −4 −2 ) available for microorganisms [11,13,14]. This fact could explain why, under these conditions, we can find hyperthermophilic archaea, which are dependent on W instead of Mo [13].…”

Section: Introductionmentioning

confidence: 99%

“…Another remarkable aspect about the relationship between Mo and W (and directly related to their chemical similarity) is the fact that some enzymes, such as DMSO reductases, can use W instead of Mo in their cofactors when Mo is at lower concentration. It is probably due to the similarity between W cofactor (WCo, tungsten-enzymes) and Mo cofactor (MoCo, molybdoenzymes) [1,11,13,15]. However, some enzymes (even in the same family) can only use one or the other despite their similarities, so the discrimination mechanism in these enzymes would be very efficient [1,13].…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

DMSO Reductase Family: Phylogenetics and Applications of Extremophiles

Miralles-Robledillo

Torregrosa-Crespo

Martínez‐Espinosa

et al. 2019

IJMS

View full text Add to dashboard Cite

Dimethyl sulfoxide reductases (DMSO) are molybdoenzymes widespread in all domains of life. They catalyse not only redox reactions, but also hydroxylation/hydration and oxygen transfer processes. Although literature on DMSO is abundant, the biological significance of these enzymes in anaerobic respiration and the molecular mechanisms beyond the expression of genes coding for them are still scarce. In this review, a deep revision of the literature reported on DMSO as well as the use of bioinformatics tools and free software has been developed in order to highlight the relevance of DMSO reductases on anaerobic processes connected to different biogeochemical cycles. Special emphasis has been addressed to DMSO from extremophilic organisms and their role in nitrogen cycle. Besides, an updated overview of phylogeny of DMSOs as well as potential applications of some DMSO reductases on bioremediation approaches are also described.

show abstract

Section: Families Of Enzymes Containing Molybdenum or Tungstenmentioning

confidence: 97%

Section: Families Of Enzymes Containing Molybdenum or Tungstenmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

DMSO Reductase Family: Phylogenetics and Applications of Extremophiles

Miralles-Robledillo

Torregrosa-Crespo

Martínez‐Espinosa

et al. 2019

IJMS

View full text Add to dashboard Cite

show abstract

Molybdenum‐Copper Antagonism In Metalloenzymes And Anti‐Copper Therapy

Maiti,

Moura,

Moura

2024

ChemBioChem

Self Cite

View full text Add to dashboard Cite

The connection between 3d (Cu) and 4d (Mo) via the “Mo‐S‐Cu” unit is called Mo‐Cu antagonism. Biology offers case studies of such interactions in metalloproteins such as Mo/Cu‐CO Dehydrogenases (Mo/Cu‐CODH), and Mo/Cu Orange Protein (Mo/Cu‐ORP). The CODH significantly maintains the CO level in the atmosphere below the toxic level by converting it to non‐toxic CO2 for respiring organisms. Several model studies were synthesized to understand the structure‐function relationship of these native enzymes. However, this interaction was first observed in ruminants, and they convert molybdate (MoO42–) into tetrathiomolybdate (MoS42–; TTM), reacting with cellular Cu to yield biological unavailable Mo/S/Cu cluster, then developing Cu‐deficiency diseases. These findings inspire the use of TTM as a Cu‐sequester drug, especially for treating Cu‐dependent human diseases such as Wilson diseases (WD) and cancer. It is well known that a balanced Cu homeostasis is essential for a wide range of biological processes, but negative consequence leads to cell toxicity. Therefore, this review aims to connect the Mo‐Cu antagonism in metalloproteins and anti‐copper therapy.

show abstract

Carbon Dioxide Utilisation—The Formate Route

Maia

Moura

2020

Enzymes for Solving Humankind's Problems

Self Cite

View full text Add to dashboard Cite

The relentless rise of atmospheric CO2 is causing large and unpredictable impacts on the Earth climate, due to the CO2 significant greenhouse effect, besides being responsible for the ocean acidification, with consequent huge impacts in our daily lives and in all forms of life. To stop spiral of destruction, we must actively reduce the CO2 emissions and develop new and more efficient “CO2 sinks”. We should be focused on the opportunities provided by exploiting this novel and huge carbon feedstock to produce de novo fuels and added-value compounds. The conversion of CO2 into formate offers key advantages for carbon recycling, and formate dehydrogenase (FDH) enzymes are at the centre of intense research, due to the “green” advantages the bioconversion can offer, namely substrate and product selectivity and specificity, in reactions run at ambient temperature and pressure and neutral pH. In this chapter, we describe the remarkable recent progress towards efficient and selective FDH-catalysed CO2 reduction to formate. We focus on the enzymes, discussing their structure and mechanism of action. Selected promising studies and successful proof of concepts of FDH-dependent CO2 reduction to formate and beyond are discussed, to highlight the power of FDHs and the challenges this CO2 bioconversion still faces.

show abstract

CHAPTER 1. Molybdenum and Tungsten-Containing Enzymes: An Overview

Cited by 36 publications

References 304 publications

DMSO Reductase Family: Phylogenetics and Applications of Extremophiles

DMSO Reductase Family: Phylogenetics and Applications of Extremophiles

Molybdenum‐Copper Antagonism In Metalloenzymes And Anti‐Copper Therapy

Carbon Dioxide Utilisation—The Formate Route

Contact Info

Product

Resources

About