Sulfite Oxidase
editStructure
editThe molybdenum centre has a square pyramidal geometry and is distinguished from the xanthine oxidase family by the orientation of the oxo group facing downwards rather than up.
Vertebrates
editX-ray crystallography has confirmed the structure of sulfite oxidase enzymes from chickens[1]. It is a homodimer with two N-terminal heme groups that are very similar in structure and sequence to that of cytochrome b5. Each domain is connected via a 12-15 long amino acid chain to the molybdenum centre.
Plants
editX-ray crystallography has confirmed the structure of sulfite oxidase enzymes from A. thaliana[1]. This enzyme is similar in structure to that of vertebrates but does not contain the heme domain, making the molybdenum centre the only redox active site.
Mechanism
editElectrons are passed one at a time from the molybdenum to the heme group which reacts with cytochrome c to reoxidize the enzyme. The electrons from this reaction enter the electron transport chain (ETC).
Reductive half reaction
editThis reaction is generally the rate limiting reaction. Upon reaction of the enzyme with sulfite, it is reduced by 2 electrons. The negative potential seen with re-reduction of the enzyme shows the oxidized state is favoured.
Oxidative half reaction
editAmong the Mo enzyme classes, sulfite oxidase is the most easily oxidized. Although under low pH conditions the oxidative reaction become partially rate limiting.
- ^ a b Hille, Russ; Nishino, Takeshi; Bittner, Florian (2011-05). "Molybdenum enzymes in higher organisms". Coordination Chemistry Reviews. 255 (9–10): 1179–1205. doi:10.1016/j.ccr.2010.11.034.
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Week3 Tasks - Info for Methyl Oleate
editProperties of Methyl Oleate
edit- Molecular formula: C19H36O2
- Molar mass: 296.49 g/mol
- Melting point: -20 °C
- Boiling point: 350 °C
- Solubility in water: insoluble
Methyl Oleate
Methyl Oleate
Internal link: Oleic acid
External link: Fischer Scientific - Methyl Oleate [1]
Energy Transduction in Nitrogenase [1]
Biosynthesis of Nitrogenase Metalloclusters [2]
Nitrogenase assembly [3]
- ^ Seefeldt, Lance C.; Hoffman, Brian M.; Peters, John W.; Raugei, Simone; Beratan, David N.; Antony, Edwin; Dean, Dennis R. (2018-08-10). "Energy Transduction in Nitrogenase". Accounts of Chemical Research. 51 (9): 2179–2186. doi:10.1021/acs.accounts.8b00112. ISSN 0001-4842.
- ^ Ribbe, Markus W.; Hu, Yilin; Hodgson, Keith O.; Hedman, Britt (2013-12-13). "Biosynthesis of Nitrogenase Metalloclusters". Chemical Reviews. 114 (8): 4063–4080. doi:10.1021/cr400463x. ISSN 0009-2665.
- ^ Hu, Yilin; Ribbe, Markus W. (2013-08). "Nitrogenase assembly". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1827 (8–9): 1112–1122. doi:10.1016/j.bbabio.2012.12.001. ISSN 0005-2728.
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Practice Uploading a PDB Structure Image
edit
Critique of Carbonic Anhydrase Mechanism Figure
editThe mechanism does not look professionally drawn. Not all bond lengths are equal or in the right orientation. The arrows are not a good size and specifically the arrow showing water being added is not properly drawn.
Molecular formula | C19H36O2 |
Molar mass | 296.49 g/mol |
Solubility in water | insoluble |