caa a22 4500 605507996 CHVBK 20210128100634.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1234-2 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1234-2 Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases [Elektronische Daten] [Luisa Maia, José Moura] Nitric oxide (NO) is a signalling molecule involved in several physiological processes, in both prokaryotes and eukaryotes, and nitrite is being recognised as an NO source particularly relevant to cell signalling and survival under challenging conditions. The "non-respiratory” nitrite reduction to NO is carried out by "non-dedicated” nitrite reductases, making use of metalloproteins present in cells to carry out other functions, such as several molybdoenzymes (a new class of nitric oxide-forming nitrite reductases). This minireview will highlight the physiological relevance of molybdenum-dependent nitrite-derived NO formation in mammalian, plant and bacterial signalling (and other) pathways. The mammalian xanthine oxidase/xanthine dehydrogenase, aldehyde oxidase, mitochondrial amidoxime-reducing component, plant nitrate reductase and bacterial aldehyde oxidoreductase and nitrate reductases will be considered. The nitrite reductase activity of each molybdoenzyme will be described and the review will be oriented to discuss the feasibility of the reactions from a (bio)chemical point of view. In addition, the molecular mechanism proposed for the molybdenum-dependent nitrite reduction will be discussed in detail. SBIC, 2015 Molybdenum nationallicence Nitrite reduction nationallicence Nitric oxide nationallicence Cell signalling nationallicence Moonlighting nationallicence AO : Aldehyde oxidase nationallicence AOR : Aldehyde oxidoreductases nationallicence CuNiR : Copper-containing nitrite reductase (one of the enzymes responsible for the respiratory nitrite reduction to NO) nationallicence DMSOR : Dimethylsulphoxide reductase nationallicence DPI : Diphenyleneiodonium chloride nationallicence EPR : Electron paramagnetic resonance spectroscopy nationallicence Fe/S : Iron-sulphur centre nationallicence mARC : Mammalian mitochondrial amidoxime-reducing component nationallicence MOSC : From molybdenum cofactor sulphurase C-terminal domain (proteins involved in pyranopterin cofactor biosynthesis) nationallicence NaR : Nitrate reductase (all types of nitrate reductase enzymes) nationallicence NiR : Nitrite reductases ("dedicated” and "non-dedicated” enzymes) nationallicence NO : Nitric oxide radical nationallicence NOS : NO synthases nationallicence ROS : Reactive oxygen species nationallicence SO : Sulphite oxidase nationallicence SOD : Superoxide dismutase nationallicence XD : Xanthine dehydrogenase nationallicence XO : Xanthine oxidase nationallicence Maia Luisa UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut Moura José UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 403-433 0949-8257 20:2<403 2015 20 775 https://doi.org/10.1007/s00775-014-1234-2 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1234-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Maia Luisa UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut NATIONALLICENCE 700 1- Moura José UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 403-433 0949-8257 20:2<403 2015 20 775