2I7F

Sphingomonas yanoikuyae B1 ferredoxin

Summary for 2I7F

• Entry DOI: 10.2210/pdb2i7f/pdb
• Related: 1fqt 1sjg 1vck
• Descriptor: Ferredoxin component of dioxygenase, SULFATE ION, FE2/S2 (INORGANIC) CLUSTER, ... (5 entities in total)
• Functional Keywords: rieske ferredoxin, oxidoreductase
• Biological source: Sphingobium yanoikuyae
• Total number of polymer chains: 2
• Total formula weight: 24162.37

Authors

Ramaswamy, S.,Brown, E.N. (deposition date: 2006-08-30, release date: 2007-03-20, Last modification date: 2023-08-30)

Primary citation

Ferraro, D.J.,Brown, E.N.,Yu, C.L.,Parales, R.E.,Gibson, D.T.,Ramaswamy, S.
Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1.
Bmc Struct.Biol., 7:10-10, 2007

PubMed Abstract: The initial step involved in oxidative hydroxylation of monoaromatic and polyaromatic compounds by the microorganism Sphingobium yanoikuyae strain B1 (B1), previously known as Sphingomonas yanoikuyae strain B1 and Beijerinckia sp. strain B1, is performed by a set of multiple terminal Rieske non-heme iron oxygenases. These enzymes share a single electron donor system consisting of a reductase and a ferredoxin (BPDO-FB1). One of the terminal Rieske oxygenases, biphenyl 2,3-dioxygenase (BPDO-OB1), is responsible for B1's ability to dihydroxylate large aromatic compounds, such as chrysene and benzo[a]pyrene.

PubMed: 17349044
DOI: 10.1186/1472-6807-7-10

Experimental method

X-RAY DIFFRACTION (1.9 Å)