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Literature summary for 1.15.1.2 extracted from

  • Horch, M.; Pinto, A.; Mroginski, M.; Teixeira, M.; Hildebrandt, P.; Zebger, I.
    Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase (2014), RSC Adv., 4, 54091-54095 .
No PubMed abstract available
Search for more literature for 1.15.1.2

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis, PDB ID 4BK8, modeling Ignicoccus hospitalis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a non-heme iron enzyme, catalytic Fe2+ binding residues are H25, H50, H56, C109, and H112, metal binding site structure, overview Ignicoccus hospitalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
superoxide + reduced acceptor + 2 H+ Ignicoccus hospitalis
-
 H2O2 + oxidized acceptor
-
 ?
superoxide + reduced acceptor + 2 H+ Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125
-
 H2O2 + oxidized acceptor
-
 ?

Organism

Organism UniProt Comment Textmining
Ignicoccus hospitalis A8AC72
-
-
Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 A8AC72
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
superoxide + reduced acceptor + 2 H+
-
 Ignicoccus hospitalis H2O2 + oxidized acceptor
-
 ?
superoxide + reduced acceptor + 2 H+
-
 Ignicoccus hospitalis KIN4/I / DSM 18386 / JCM 14125 H2O2 + oxidized acceptor
-
 ?

Synonyms

Synonyms Comment Organism
SOR
-
 Ignicoccus hospitalis

General Information

General Information Comment Organism
evolution based on the number of metal centres, superoxide reductases can be divided into two major subclasses: neelaredoxins (Nlr) solely contain the active site (1Fe-SOR), while desulfoferrodoxins (Dfx) harbour an additional rubredoxin-like iron centre (2Fe-SOR) Ignicoccus hospitalis
additional information Superoxide reductases form a group of non-heme iron enzymes that supply one electron during substrate reduction. In the ferrous state, the active site iron is coordinated by four equatorial histidines and an axial cysteinate, forming a square pyramidal geometry with a vacant site for substrate binding. In the octahedral ferric state, coordination of the active site is not uniform: during turnover, the sixth coordination site is supposedly occupied by dioxygen species in different protonation and oxidation states. In contrast, the ferric resting state comprises an additional glutamate as a ligand in most, but not all, cases. Metal binding site and active site structure analysis, overview Ignicoccus hospitalis