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Sulfite Oxidase
[edit]Structure
[edit]The 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
[edit]X-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
[edit]X-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
[edit]Electrons 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
[edit]This 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
[edit]Among 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
[edit]Properties 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
[edit]The 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 |