The amino acid sequence of desulforedoxin, a new type of non heme iron protein from Desulfovibrio gigas

1979 ◽  
Vol 90 (2) ◽  
pp. 596-605 ◽  
Author(s):  
M. Bruschi ◽  
I. Moura ◽  
J. Le Gall ◽  
A.V. Xavier ◽  
L.C. Sieker
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heme Iron ◽  
Iron Protein ◽  
Desulfovibrio Gigas ◽  
Non Heme Iron ◽  
New Type

scholarly journals Novel Three-Component Rieske Non-Heme Iron Oxygenase System Catalyzing theN-Dealkylation of Chloroacetanilide Herbicides in Sphingomonads DC-6 and DC-2

2014 ◽  
Vol 80 (16) ◽  
pp. 5078-5085 ◽  
Author(s):  
Qing Chen ◽  
Cheng-Hong Wang ◽  
Shi-Kai Deng ◽  
Ya-Dong Wu ◽  
Yi Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heme Iron ◽  
Content Type ◽  
Non Heme Iron ◽  
Transport Component ◽  
Reductase Gene ◽  
Chloroacetanilide Herbicides ◽  
The Individual ◽  
Sequence Identities

ABSTRACTSphingomonads DC-6 and DC-2 degrade the chloroacetanilide herbicides alachlor, acetochlor, and butachlor viaN-dealkylation. In this study, we report a three-component Rieske non-heme iron oxygenase (RHO) system catalyzing theN-dealkylation of these herbicides. The oxygenase component genecndAis located in a transposable element that is highly conserved in the two strains. CndA shares 24 to 42% amino acid sequence identities with the oxygenase components of some RHOs that catalyzeN- orO-demethylation. Two putative [2Fe-2S] ferredoxin genes and one glutathione reductase (GR)-type reductase gene were retrieved from the genome of each strain. These genes were not located in the immediate vicinity ofcndA. The four ferredoxins share 64 to 72% amino acid sequence identities to the ferredoxin component of dicambaO-demethylase (DMO), and the two reductases share 62 to 65% amino acid sequence identities to the reductase component of DMO.cndA, the four ferredoxin genes, and the two reductases genes were expressed inEscherichia coli, and the recombinant proteins were purified using Ni-affinity chromatography. The individual components or the components in pairs displayed no activity; the enzyme mixture showedN-dealkylase activities toward alachlor, acetochlor, and butachlor only when CndA-His6was combined with one of the four ferredoxins and one of the two reductases, suggesting that the enzyme consists of three components, a homo-oligomer oxygenase, a [2Fe-2S] ferredoxin, and a GR-type reductase, and CndA has a low specificity for the electron transport component (ETC). TheN-dealkylase utilizes NADH, but not NADPH, as the electron donor.

A Blue Non-Heme Iron Protein from Desulfovibrio gigas

1994 ◽  
Vol 226 (2) ◽  
pp. 613-618 ◽  
Author(s):  
Liang Chen ◽  
Pardeep Sharma ◽  
Jean Gall ◽  
Aida M. Mariano ◽  
Miguel Teixeira ◽  
...  
Keyword(s):  
Heme Iron ◽  
Iron Protein ◽  
Desulfovibrio Gigas ◽  
Non Heme Iron

The Structure of a Non-Heme Iron Protein: Rubredoxin at 1.5 A Resolution

1972 ◽  
Vol 36 (0) ◽  
pp. 359-367 ◽  
Author(s):  
K. D. Watenpaugh ◽  
L. C. Sieker ◽  
J. R. Herriott ◽  
L. H. Jensen
Keyword(s):  
Heme Iron ◽  
Iron Protein ◽  
Non Heme Iron
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