1H1O

Acidithiobacillus ferrooxidans cytochrome c4 structure supports a complex-induced tuning of electron transfer

Summary for 1H1O

• Entry DOI: 10.2210/pdb1h1o/pdb
• Descriptor: CYTOCHROME C-552, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (6 entities in total)
• Functional Keywords: electron transport, c4, cytochrome, electron transfer, heme
• Biological source: THIOBACILLUS FERROOXIDANS
• Cellular location: Periplasm: P74917
• Total number of polymer chains: 2
• Total formula weight: 43015.85

Authors

Abergel, C.,Nitschke, W.,Malarte, G.,Bruschi, M.,Claverie, J.-M.,Guidici-Orticoni, M.-T. (deposition date: 2002-07-19, release date: 2003-07-17, Last modification date: 2024-05-08)

Primary citation

Abergel, C.,Nitschke, W.,Malarte, G.,Bruschi, M.,Claverie, J.-M.,Guidici-Orticoni, M.-T.
The Structure of Acidithiobacillus Ferrooxidans C(4)-Cytochrome. A Model for Complex-Induced Electron Transfer Tuning
Structure, 11:547-, 2003

PubMed Abstract: The study of electron transfer between the copper protein rusticyanin (RCy) and the c(4)-cytochrome CYC(41) of the acidophilic bacterium Acidithiobacillus ferrooxidans has evidenced a remarkable decrease of RCy's redox potential upon complex formation. The structure of the CYC(41) obtained at 2.2 A resolution highlighted a specific glutamate residue (E121) involved in zinc binding as potentially playing a central role in this effect, required for the electron transfer to occur. EPR and stopped-flow experiments confirmed the strong inhibitory effect of divalent cations on CYC(41):RCy complex formation. A docking analysis of the CYC(41) and RCy structure allows us to propose a detailed model for the complex-induced tuning of electron transfer in agreement with our experimental data, which could be representative of other copper proteins involved in electron transfer.

PubMed: 12737820
DOI: 10.1016/S0969-2126(03)00072-8

Experimental method

X-RAY DIFFRACTION (2.13 Å)