F. E. Dodd
Daresbury Laboratory
17 Papers
268 Citations
F. E. Dodd is an academic researcher from Daresbury Laboratory. The author has contributed to research in topics: Nitrite reductase & Azurin. The author has an hindex of 13, co-authored 17 publications. Previous affiliations of F. E. Dodd include De Montfort University.
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Papers
Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu.
TL;DR: The first atomic resolution (<1.20 A) structure of a copper protein, nitrite reductase, and of a mutant of the catalytically important Asp92 residue (D92E) is provided, providing the basis from which to build a detailed mechanism of this important enzyme.
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The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase
Richard W. Strange,F. E. Dodd,F. E. Dodd,Z. H. L. Abraham,J. Günter Grossmann,Thomas Brüser,Robert R. Eady,Barry E. Smith,S. Samar Hasnain +8 more
TL;DR: Modelling suggests a similarity between this unusual type-2 Cu site in nitrite reductase and the Zn site in carbonic anhydrase and that nitrite is anchored by hydrogen bonds to an unligated histidine present in the type-1 Cu cavity.
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Evidence for Two Distinct Azurins in Alcaligenes xylosoxidans (NCIMB 11015): Potential Electron Donors to Nitrite Reductase
F. E. Dodd,S. Samar Hasnain,William N. Hunter,Z. H. L. Abraham,Michael Debenham,Holger Kanzler,M E Eldridge,Robert R. Eady,Richard P. Ambler,Barry E. Smith +9 more
TL;DR: Two type 1 copper-containing proteins from Alcaligenes xylosoxidans (NCIMB 11015) grown under denitrifying conditions are isolated and are shown to be the previously identified azurin (Ambler, 1971) and a related, but previously undescribed, blue copper protein, which is proposed to be an Azurin II.
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Electron donation between copper containing nitrite reductases and cupredoxins: the nature of protein-protein interaction in complex formation.
TL;DR: Results from the first comprehensive electron donation experiments using three copper nitrite reductases, one green and two blue, and five cupredoxins, one pseudoazurin and four azurins are reported.
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Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteins.
Lalji D. Kanbi,Svetlana V. Antonyuk,Michael A. Hough,John F. Hall,F. E. Dodd,S. Samar Hasnain,S. Samar Hasnain +6 more
TL;DR: In this paper, the crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin are presented at 1.82 and 1.65 A resolution, respectively.
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