Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605507996 | ||
| 003 | CHVBK | ||
| 005 | 20210128100634.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20150301xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00775-014-1234-2 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-014-1234-2 | ||
| 245 | 0 | 0 | |a Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases |h [Elektronische Daten] |c [Luisa Maia, José Moura] |
| 520 | 3 | |a 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. | |
| 540 | |a SBIC, 2015 | ||
| 690 | 7 | |a Molybdenum |2 nationallicence | |
| 690 | 7 | |a Nitrite reduction |2 nationallicence | |
| 690 | 7 | |a Nitric oxide |2 nationallicence | |
| 690 | 7 | |a Cell signalling |2 nationallicence | |
| 690 | 7 | |a Moonlighting |2 nationallicence | |
| 690 | 7 | |a AO : Aldehyde oxidase |2 nationallicence | |
| 690 | 7 | |a AOR : Aldehyde oxidoreductases |2 nationallicence | |
| 690 | 7 | |a CuNiR : Copper-containing nitrite reductase (one of the enzymes responsible for the respiratory nitrite reduction to NO) |2 nationallicence | |
| 690 | 7 | |a DMSOR : Dimethylsulphoxide reductase |2 nationallicence | |
| 690 | 7 | |a DPI : Diphenyleneiodonium chloride |2 nationallicence | |
| 690 | 7 | |a EPR : Electron paramagnetic resonance spectroscopy |2 nationallicence | |
| 690 | 7 | |a Fe/S : Iron-sulphur centre |2 nationallicence | |
| 690 | 7 | |a mARC : Mammalian mitochondrial amidoxime-reducing component |2 nationallicence | |
| 690 | 7 | |a MOSC : From molybdenum cofactor sulphurase C-terminal domain (proteins involved in pyranopterin cofactor biosynthesis) |2 nationallicence | |
| 690 | 7 | |a NaR : Nitrate reductase (all types of nitrate reductase enzymes) |2 nationallicence | |
| 690 | 7 | |a NiR : Nitrite reductases ("dedicated” and "non-dedicated” enzymes) |2 nationallicence | |
| 690 | 7 | |a NO : Nitric oxide radical |2 nationallicence | |
| 690 | 7 | |a NOS : NO synthases |2 nationallicence | |
| 690 | 7 | |a ROS : Reactive oxygen species |2 nationallicence | |
| 690 | 7 | |a SO : Sulphite oxidase |2 nationallicence | |
| 690 | 7 | |a SOD : Superoxide dismutase |2 nationallicence | |
| 690 | 7 | |a XD : Xanthine dehydrogenase |2 nationallicence | |
| 690 | 7 | |a XO : Xanthine oxidase |2 nationallicence | |
| 700 | 1 | |a Maia |D Luisa |u UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | |
| 700 | 1 | |a Moura |D José |u UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 403-433 |x 0949-8257 |q 20:2<403 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1234-2 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a review-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-014-1234-2 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Maia |D Luisa |u UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Moura |D José |u UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 403-433 |x 0949-8257 |q 20:2<403 |1 2015 |2 20 |o 775 | ||