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Iron oxidation state modulates active site structure in a heme peroxidase.

Abstract:

We have previously shown [Badyal, S. K., et al. (2006) J. Biol. Chem. 281, 24512-24520] that the distal histidine (His42) in the W41A variant of ascorbate peroxidase binds to the heme iron in the ferric form of the protein but that binding of the substrate triggers a conformational change in which His42 dissociates from the heme. In this work, we show that this conformational rearrangement also occurs upon reduction of the heme iron. Thus, we present X-ray crystallographic data to show that r...

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Publication status:
Published

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Publisher copy:
10.1021/bi702337n

Authors


Badyal, SK More by this author
Metcalfe, CL More by this author
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Journal:
Biochemistry
Volume:
47
Issue:
15
Pages:
4403-4409
Publication date:
2008-04-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:7a381d16-e640-4d58-a88e-0e07ff8d53c3
Source identifiers:
240692
Local pid:
pubs:240692

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