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pH dependence of co...
pH dependence of copper geometry, reduction potential, and nitrite affinity in nitrite reductase
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- Jacobson, Frida, 1975 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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Pistorius, A. (author)
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- Farkas, Daniel, 1980 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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De Grip, W. (author)
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- Hansson, Örjan, 1955 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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- Sjölin, Lennart, 1949 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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- Neutze, Richard, 1969 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi,Department of Chemistry,University of Gothenburg
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(creator_code:org_t)
- 2007
- 2007
- English.
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In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 282:9, s. 6347-6355
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Abstract
Subject headings
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- Many properties of copper-containing nitrite reductase are pH-dependent, such as gene expression, enzyme activity, and substrate affinity. Here we use x-ray diffraction to investigate the structural basis for the pH dependence of activity and nitrite affinity by examining the type 2 copper site and its immediate surroundings in nitrite reductase from Rhodobacter sphaeroides 2.4.3. At active pH the geometry of the substrate-free oxidized type 2 copper site shows a near perfect tetrahedral geometry as defined by the positions of its ligands. At higher pH values the most favorable copper site geometry is altered toward a more distorted tetrahedral geometry whereby the solvent ligand adopts a position opposite to that of the His-131 ligand. This pH-dependent variation in type 2 copper site geometry is discussed in light of recent computational results. When co-crystallized with substrate, nitrite is seen to bind in a bidentate fashion with its two oxygen atoms ligating the type 2 copper, overlapping with the positions occupied by the solvent ligand in the high and low pH structures. Fourier transformation infrared spectroscopy is used to assign the pH dependence of the binding of nitrite to the active site, and EPR spectroscopy is used to characterize the pH dependence of the reduction potential of the type 2 copper site. Taken together, these spectroscopic and structural observations help to explain the pH dependence of nitrite reductase, highlighting the subtle relationship between copper site geometry, nitrite affinity, and enzyme activity.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Kemiteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Chemical Engineering (hsv//eng)
Keyword
- ALCALIGENES-FAECALIS S-6
- X-RAY-STRUCTURE
- INTRAMOLECULAR
- ELECTRON-TRANSFER
- ATOMIC-RESOLUTION STRUCTURES
- TYPE-2 COPPER
- ACHROMOBACTER-CYCLOCLASTES
- ACTIVE-SITE
- MOLECULAR REPLACEMENT
- ANGSTROM RESOLUTION
- SUBSTRATE-BINDING
- ACTIVE-SITE
Publication and Content Type
- ref (subject category)
- art (subject category)
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Jacobson, Frida, ...
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Pistorius, A.
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Farkas, Daniel, ...
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De Grip, W.
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Hansson, Örjan, ...
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Sjölin, Lennart, ...
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show more...
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Neutze, Richard, ...
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- About the subject
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- ENGINEERING AND TECHNOLOGY
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ENGINEERING AND ...
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and Chemical Enginee ...
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Journal of Biolo ...
- By the university
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University of Gothenburg
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Chalmers University of Technology