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Sulfite Oxidase[edit]

Structure of the molybdenum centre of sulfite oxidase enzymes

Structure[edit]

The pyranopterin ligand which coordinates the molybdenum centre via the enedithiolate

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]

Structure of sulfite oxidase isolated from chicken liver

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.

Molybdenum active site of sulfite oxidase from chicken liver
Heme site in sulfite oxidase from chicken liver

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.


Structure of sulfite oxidase isolated from A. thaliana
Active site in sulfite oxidase from A. thaliana
  1. ^ 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. {{cite journal}}: Check date values in: |date= (help)




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]

  1. ^ 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.
  2. ^ 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.
  3. ^ 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. {{cite journal}}: Check date values in: |date= (help)

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.

Table of Properties of Methyl Oleate
Molecular formula C19H36O2
Molar mass 296.49 g/mol
Solubility in water insoluble


Practice Using History Pages, Talk pages, Article ratings and Watchlists[edit]