Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology
Luisa B Maia, Biplab K Maiti, Isabel Moura, José J G Moura
Molecules, doi:10.3390/molecules29010120
Living organisms use selenium mainly in the form of selenocysteine in the active site of oxidoreductases. Here, selenium's unique chemistry is believed to modulate the reaction mechanism and enhance the catalytic efficiency of specific enzymes in ways not achievable with a sulfur-containing cysteine. However, despite the fact that selenium/sulfur have different physicochemical properties, several selenoproteins have fully functional cysteine-containing homologues and some organisms do not use selenocysteine at all. In this review, selected selenocysteine-containing proteins will be discussed to showcase both situations: (i) selenium as an obligatory element for the protein's physiological function, and (ii) selenium presenting no clear advantage over sulfur (functional proteins with either selenium or sulfur). Selenium's physiological roles in antioxidant defence (to maintain cellular redox status/hinder oxidative stress), hormone metabolism, DNA synthesis, and repair (maintain genetic stability) will be also highlighted, as well as selenium's role in human health. Formate dehydrogenases, hydrogenases, glutathione peroxidases, thioredoxin reductases, and iodothyronine deiodinases will be herein featured.
Abbreviations ACE-2: angiotensin-converting enzyme 2; COVID-19, Coronavirus Disease-2019; Cys-FDH, cysteine-containing FDH; Cys-FMFDH, cysteine-containing FMFDH; Cys-Mo-FDH, cysteine and molybdenum-containing FDH; Cys-W-FDH, cysteine and tungsten-containing FDH; Dios, iodothyronine deiodinases; DM, diabetes mellitus; EPR, electron paramagnetic resonance spectroscopy; FDH, formate dehydrogenase; [Fe]-Hase, [Fe]-hydrogenase; [FeFe]-Hase, [FeFe]-hydrogenases; FMFDH, Nformyl-methanofuran dehydrogenases; GPx, glutathione peroxidase; GSH, glutathione; Hase, hydrogenases; HIV, human immunodeficiency virus; IRD, inner-ring deiodination; Mpro, main proteases; [NiFe]-Hase, [NiFe]-hydrogenase; [NiSeFe]-Hase, [NiSeFe]-hydrogenase; ORD, outer-ring deiodination; ROS, reactive oxygen species; R-SeOH, selenenic acid; R-SeOOH, seleninic acid; SARS-CoV-2, severe acute respiratory syndrome coronavirus 2; SeCys-FDH, selenocysteine-containing FDH; SeCys-FMFDH, selebocysteine-containing FMFDH; SeCys-Mo-FDH, selenocysteine and molybdenumcontaining FDH; SeCys-W-FDH, selenocysteine and tungsten-containing FDH; SePs, selenoproteins; T2DM, Type 2 diabetes mellitus; TGR, thioredoxin glutathione reductase; Trx, thioredoxin; TrxR, thioredoxin reductase; XAS, X-ray absorption spectroscopy.
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doi:10.1073/pnas.83.13.4650{ 'indexed': { 'date-parts': [[2023, 12, 27]],
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'abstract': '<jats:p>Living organisms use selenium mainly in the form of selenocysteine in the active site '
'of oxidoreductases. Here, selenium’s unique chemistry is believed to modulate the reaction '
'mechanism and enhance the catalytic efficiency of specific enzymes in ways not achievable '
'with a sulfur-containing cysteine. However, despite the fact that selenium/sulfur have '
'different physicochemical properties, several selenoproteins have fully functional '
'cysteine-containing homologues and some organisms do not use selenocysteine at all. In this '
'review, selected selenocysteine-containing proteins will be discussed to showcase both '
'situations: (i) selenium as an obligatory element for the protein’s physiological function, '
'and (ii) selenium presenting no clear advantage over sulfur (functional proteins with either '
'selenium or sulfur). Selenium’s physiological roles in antioxidant defence (to maintain '
'cellular redox status/hinder oxidative stress), hormone metabolism, DNA synthesis, and repair '
'(maintain genetic stability) will be also highlighted, as well as selenium’s role in human '
'health. Formate dehydrogenases, hydrogenases, glutathione peroxidases, thioredoxin '
'reductases, and iodothyronine deiodinases will be herein featured.</jats:p>',
'DOI': '10.3390/molecules29010120',
'type': 'journal-article',
'created': { 'date-parts': [[2023, 12, 25]],
'date-time': '2023-12-25T01:42:30Z',
'timestamp': 1703468550000},
'page': '120',
'source': 'Crossref',
'is-referenced-by-count': 0,
'title': 'Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology',
'prefix': '10.3390',
'volume': '29',
'author': [ { 'ORCID': 'http://orcid.org/0000-0002-6901-6591',
'authenticated-orcid': False,
'given': 'Luisa B.',
'family': 'Maia',
'sequence': 'first',
'affiliation': [ { 'name': 'LAQV, REQUIMTE, Department of Chemistry, NOVA School of Science '
'and Technology | NOVA FCT, 2829-516 Caparica, Portugal'}]},
{ 'ORCID': 'http://orcid.org/0000-0002-0985-0031',
'authenticated-orcid': False,
'given': 'Biplab K.',
'family': 'Maiti',
'sequence': 'additional',
'affiliation': [ { 'name': 'Department of Chemistry, School of Sciences, Cluster University '
'of Jammu, Canal Road, Jammu 180001, India'}]},
{ 'given': 'Isabel',
'family': 'Moura',
'sequence': 'additional',
'affiliation': [ { 'name': 'LAQV, REQUIMTE, Department of Chemistry, NOVA School of Science '
'and Technology | NOVA FCT, 2829-516 Caparica, Portugal'}]},
{ 'ORCID': 'http://orcid.org/0000-0002-4726-2388',
'authenticated-orcid': False,
'given': 'José J. G.',
'family': 'Moura',
'sequence': 'additional',
'affiliation': [ { 'name': 'LAQV, REQUIMTE, Department of Chemistry, NOVA School of Science '
'and Technology | NOVA FCT, 2829-516 Caparica, Portugal'}]}],
'member': '1968',
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