Do multiheme cytochromes containing close-packed heme groups have a band structure formed from the heme π and π* orbitals?

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F24%3A43908495" target="_blank" >RIV/60076658:12310/24:43908495 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S2451910324001170?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S2451910324001170?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.coelec.2024.101556" target="_blank" >10.1016/j.coelec.2024.101556</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Do multiheme cytochromes containing close-packed heme groups have a band structure formed from the heme π and π* orbitals?

Popis výsledku v původním jazyce

Multiheme cytochromes (MHCs) are bacterial electron-transfer proteins. We show from optical spectra and calculations that some of these cytochromes probably contain occupied and unoccupied bands formed from heme Tc and Tc* orbitals that span the protein. In the fully oxidised proteins, the unoccupied Tc*-bands are energetically above the redox-active frontier orbitals, which according to NMR data and calculations, are formed of Fe3+ t2g and porphyrin Tc-orbitals. These orbitals on different hemes are electronically coupled according to EPR data and calculations, but only weakly so. We suggest a role for the heme bands in the electronic conductivity of single MHCs in bioelectronic junctions that is distinct from the role of the redox-active Fe3+ t2g and porphyrin Tc-orbitals in physiological electron transfer.

Název v anglickém jazyce

Do multiheme cytochromes containing close-packed heme groups have a band structure formed from the heme π and π* orbitals?

Popis výsledku anglicky

Multiheme cytochromes (MHCs) are bacterial electron-transfer proteins. We show from optical spectra and calculations that some of these cytochromes probably contain occupied and unoccupied bands formed from heme Tc and Tc* orbitals that span the protein. In the fully oxidised proteins, the unoccupied Tc*-bands are energetically above the redox-active frontier orbitals, which according to NMR data and calculations, are formed of Fe3+ t2g and porphyrin Tc-orbitals. These orbitals on different hemes are electronically coupled according to EPR data and calculations, but only weakly so. We suggest a role for the heme bands in the electronic conductivity of single MHCs in bioelectronic junctions that is distinct from the role of the redox-active Fe3+ t2g and porphyrin Tc-orbitals in physiological electron transfer.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Current Opinion in Electrochemistry

ISSN

2451-9103

e-ISSN

2451-9103

Svazek periodika

47

Číslo periodika v rámci svazku

OCT 2024

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

—

Kód UT WoS článku

001269446800001

EID výsledku v databázi Scopus

2-s2.0-85198273206