1.13.11.49: chlorite O2-lyase
This is an abbreviated version!
For detailed information about chlorite O2-lyase, go to the full flat file.
Word Map on EC 1.13.11.49
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1.13.11.49
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perchlorate
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chlorate
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dechloromonas
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perchlorate-reducing
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dismutases
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clo2
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dismutation
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high-spin
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low-spin
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dechloratans
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defluvii
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chlorate-reducing
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nitrospira
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ideonella
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aromatica
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azospira
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hemqs
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environmental protection
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molecular biology
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biotechnology
- 1.13.11.49
- perchlorate
- chlorate
- dechloromonas
-
perchlorate-reducing
- dismutases
- clo2
-
dismutation
-
high-spin
-
low-spin
- dechloratans
- defluvii
-
chlorate-reducing
- nitrospira
- ideonella
- aromatica
- azospira
-
hemqs
- environmental protection
- molecular biology
- biotechnology
Reaction
Synonyms
chlorite dismutase, CLD, Cyan7425_1434, dimutase, chlorite, HemQ, Pfam chlorite dismutase, PitA
ECTree
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Metals Ions
Metals Ions on EC 1.13.11.49 - chlorite O2-lyase
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(NH4)2SO4
Stutzerimonas chloritidismutans
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activity increases with increasing salt concentration up to 2 M
Fe2+
Iron
Na2SO4
Stutzerimonas chloritidismutans
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activity increases with increasing salt concentration up to 2 M
NaClO3
Stutzerimonas chloritidismutans
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decreasing activity with increasing salt concentration
NaNO3
Stutzerimonas chloritidismutans
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decreasing activity with increasing salt concentration
potassium phosphate
Stutzerimonas chloritidismutans
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activity increases with increasing salt concentration up to 1 M salt, decrease beyond 1 M salt
Sodium phosphate
Stutzerimonas chloritidismutans
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activity increases with increasing salt concentration up to 1 M salt, decrease beyond 1 M salt
additional information
Stutzerimonas chloritidismutans
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kosmotropic salts such as sulfate and phosphate stabilize protein structures by water-structuring effects of the ions, chaotropic salts such as nitrate and chlorate reduce the activity, no effect of NaCl, NH4Cl, and NaHCO3 (up to 1.5 M) on enzyme activity
Iron
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spectroscopic evidence is presented for a proximal histidine coordinating the heme iron center of the enzyme. The bond between the proximal histidine and the iron is weak and can be broken upon binding of NO. The midpoint potential, Em (Fe3+/2+) = -23 mV
Iron
vibrational frequency correlations between either ny(FeIII-F) or ny(FeIII-OH) and ny(FeII-His) orthogonalize proximal and distal effects on the bonding between iron and exogenous pi-donor ligands
Iron
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vibrational frequency correlations between either ny(FeIII-F) or ny(FeIII-OH) and ny(FeII-His) orthogonalize proximal and distal effects on the bonding between iron and exogenous pi-donor ligands