Journal article
Evidence for Electrostatic Channeling in a Fusion Protein of Malate Dehydrogenase and Citrate Synthase
Biochemistry (Easton), Vol.35(39), pp.12652-12658
10/01/1996
DOI: 10.1021/bi9614747
PMID: 8841108
Abstract
Brownian dynamics simulations were performed to investigate a possible role for electrostatic channeling in transferring substrate between two of the enzymes of the citric acid cycle. The diffusion of oxaloacetate from one of the active sites of malate dehydrogenase (MDH) to the active sites of citrate synthase (CS) was simulated in the presence and absence of electrostatic forces using a modeled structure for a MDH−CS fusion protein. In the absence of electrostatic forces, fewer than 1% of substrate molecules leaving the MDH active site are transferred to CS. When electrostatic forces are present at zero ionic strength however, around 45% of substrate molecules are successfully channeled. As expected for an electrostatic mechanism of transfer, increasing the ionic strength in the simulations reduces the calculated transfer efficiency. Even at 150 mM however, the inclusion of electrostatic forces results in an increase in transfer efficiency of more than 1 order of magnitude. The simulations therefore provide evidence for the involvement of electrostatic channeling in guiding substrate transfer between two of the enzymes of the citric acid cycle. Similar effects may operate between other members of the citric acid metabolon.
Details
- Title: Subtitle
- Evidence for Electrostatic Channeling in a Fusion Protein of Malate Dehydrogenase and Citrate Synthase
- Creators
- Adrian H ElcockJ. Andrew McCammon
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.35(39), pp.12652-12658
- Publisher
- American Chemical Society
- DOI
- 10.1021/bi9614747
- PMID
- 8841108
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 10/01/1996
- Academic Unit
- Physics and Astronomy; Biochemistry and Molecular Biology
- Record Identifier
- 9984025293202771
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