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Nash, Benjamin W., Fernandes, Tomás M., Burton, Joshua A. J., Morgado, Leonor, van Wonderen, Jessica H., Svistunenko, Dimitri A., Edwards, Marcus J., Salgueiro, Carlos A., Butt, Julea N. 
ORCID: https://orcid.org/0000-0002-9624-5226 and Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914
(2024)
Tethered heme domains in a triheme cytochrome allow for increased electron transport distances.
Protein Science, 33 (11).
ISSN 1469-896X
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Abstract
Decades of research describe myriad redox enzymes that contain cofactors arranged in tightly packed chains facilitating rapid and controlled intra-protein electron transfer. Many such enzymes participate in extracellular electron transfer (EET), a process which allows microorganisms to conserve energy in anoxic environments by exploiting mineral oxides and other extracellular substrates as terminal electron acceptors. In this work, we describe the properties of the triheme cytochrome PgcA from Geobacter sulfurreducens. PgcA has been shown to play an important role in EET but is unusual in containing three CXXCH heme binding motifs that are separated by repeated (PT)x motifs, suggested to enhance binding to mineral surfaces. Using a combination of structural, electrochemical, and biophysical techniques, we experimentally demonstrate that PgcA adopts numerous conformations stretching as far as 180 Å between the ends of domains I and III, without a tightly packed cofactor chain. Furthermore, we demonstrate a distinct role for its domain III as a mineral reductase that is recharged by domains I and II. These findings show PgcA to be the first of a new class of electron transfer proteins, with redox centers separated by some nanometers but tethered together by flexible linkers, facilitating electron transfer through a tethered diffusion mechanism rather than a fixed, closely packed electron transfer chain.
| Item Type: | Article |
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| Additional Information: | Data Availability Statement: The data that support the findings of this study are openly available in PURE at https://research-portal.uea.ac.uk/en/datasets/nash-et-al-datasets-for-tethered-heme-domains-in-a-triheme-cytoch. Crystallographic coordinates and structure factors were deposited in the RCSB Protein Data Bank with PDB IDs 8QJ6 (Domain I), 8QJG (Domain II), and 8QK0 (Domain III). Funding information: This work was funded by the UKRI Biotechnology and Biological Sciences Research Council Norwich Research Park Biosciences Doctoral Training Partnership (Grant no. BB/T008717/1), BBSRC grant award BB/X011453/1 and Fundação para a Ciência e Tecnologia (Portugal) grants SFRH/BD/145039/2019 and COVID/BD/153449/2023 (TMF), PTDC/BIA-BQM/4967/2020 (CAS), 2021.02185.CEECIND/CP1657/CT0008 (LM), UIDP/04378/2020 and UIDB/04378/2020 (UCIBIO), and LA/P/0140/2020 (i4HB). |
| Uncontrolled Keywords: | cytochrome,electron transfer,flexibility,heme,microbe–mineral interface,biochemistry,molecular biology ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Centre for Photonics and Quantum Science Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Energy Materials Laboratory Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 18 Nov 2024 10:30 |
| Last Modified: | 27 Nov 2024 10:45 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/97705 |
| DOI: | 10.1002/pro.5200 |
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