7ZS1
Diheme cytochrome c Kustd1711 from Kuenenia stuttgartiensis, M292C mutant
Summary for 7ZS1
| Entry DOI | 10.2210/pdb7zs1/pdb |
| Descriptor | Hypothetical (Diheme) protein, CALCIUM ION, HEME C, ... (5 entities in total) |
| Functional Keywords | anaerobic ammonium oxidation, electron transport |
| Biological source | Candidatus Kuenenia |
| Total number of polymer chains | 1 |
| Total formula weight | 35808.54 |
| Authors | Akram, M.,Barends, T. (deposition date: 2022-05-05, release date: 2023-05-17, Last modification date: 2025-01-22) |
| Primary citation | Akram, M.,Hauser, D.,Dietl, A.,Steigleder, M.,Ullmann, G.M.,Barends, T.R.M. Redox potential tuning by calcium ions in a novel c-type cytochrome from an anammox organism. J.Biol.Chem., :108082-108082, 2024 Cited by PubMed Abstract: The electrochemical potentials of redox-active proteins need to be tuned accurately to the correct values for proper biological function. Here, we describe a diheme cytochrome c with high heme redox potentials of about +350 mV, despite having a large overall negative charge, which typically reduces redox potentials. High-resolution crystal structures, spectroelectrochemical measurements, and high-end computational methods show how this is achieved: each heme iron has a calcium cation positioned next to it at a distance of only 6.9 Å, raising their redox potentials by several hundred millivolts through electrostatic interaction. We suggest that this has evolved to provide the protein with a high redox potential despite its large negative surface charge, which it likely requires for interactions with redox partners. PubMed: 39675707DOI: 10.1016/j.jbc.2024.108082 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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