Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Methane monooxygenase diferrous form

Structure of the Iron Center Formation of the Iron Center and Tyrosyl Radical Spectroscopy of the Diferric Iron Center Spectroscopy of the Tyrosyl Radical Redox Properties of the Iron Center Mixed-Valent Form of the Iron Center Diferrous Form of the Iron Center Inhibitors to Iron-Containing Ribonucleotide Reductase Methane Monooxygenase A. Spectroscopy of the MMOH Cluster X-Ray Structure of MMOH... [Pg.359]

Fig. 1. Diferric iron clusters form hemer3fthrin, ribonucleotide reductase R2 subunit, and methane monooxygenase hydroxylase. The figure was made with the RasMol 2.0 program, and the protein coordinates as PDB files were obtained from Brookhaven Protein Data Bank. Only the amino acids (histidines, green carboxylates, black oxygen, red nitrogen, yellow acetate, blue iron, violet) coordinated to the iron cluster are shown, coordinated waters are not indicated. The first subunit containing the cluster is shown. Diferric Hr is from sipunculid worm Themiste dyscritra). The RNR-R2 is from E. coli. The MMOH is from Methvlococcus caosulatus (Bath). Fig. 1. Diferric iron clusters form hemer3fthrin, ribonucleotide reductase R2 subunit, and methane monooxygenase hydroxylase. The figure was made with the RasMol 2.0 program, and the protein coordinates as PDB files were obtained from Brookhaven Protein Data Bank. Only the amino acids (histidines, green carboxylates, black oxygen, red nitrogen, yellow acetate, blue iron, violet) coordinated to the iron cluster are shown, coordinated waters are not indicated. The first subunit containing the cluster is shown. Diferric Hr is from sipunculid worm Themiste dyscritra). The RNR-R2 is from E. coli. The MMOH is from Methvlococcus caosulatus (Bath).
The hydroxylase component of methane monooxygenase (MMO) contains the diiron active site (11, 12, 30, 31). The properties of the diferric form of MMO differ from those of metHr and RRB2. This enzyme is essentially colorless with an electronic spectrum that exhibits a weak absorption tail in the region of 300-400 nm (Fig. 10). It exhibits only one quadrupole doublet in the Mdssbauer spectrum with a splitting of 1.07 mm s a value that is intermediate between (p.-oxo)diiron complexes... [Pg.125]

The two-electron reduction of the diferric forms of hemerythrin (51), ribonucleotide reductase (27, 50), and methane monooxygenase (31) yields dioxygen-sensitive diferrous forms of the proteins. All three can be generated by dithionite treatment of the corresponding diferric forms, although the RRB2 reduction requires methyl viologen as mediator. The Fe(II) oxidation state is more difficult to probe spectroscopically, and only recently have methods been developed that allow this state to be characterized further. [Pg.127]


See other pages where Methane monooxygenase diferrous form is mentioned: [Pg.192]    [Pg.137]    [Pg.59]    [Pg.2003]    [Pg.2004]    [Pg.401]    [Pg.99]    [Pg.254]    [Pg.2002]    [Pg.2003]    [Pg.275]   
See also in sourсe #XX -- [ Pg.127 ]




SEARCH



Methane monooxygenase

Methane monooxygenase diferric form

Methane monooxygenase diferric form

Methane monooxygenases

Monooxygenases methan monooxygenase

© 2024 chempedia.info