
저전위 페레독신에서 [4Fe-4S] 클러스터 근처 Asp64 잔기의 양성자화 상태가 전자 전달 과정에서 환원 상태의 안정성을 제어하는 스위치 역할을 한다.


coremsg

Ferredoxin is a small iron-sulfur protein and acts as an electron carrier. Low-potential ferredoxins harbor [4Fe-4S] cluster(s), which play(s) a crucial role as the redox center. Low-potential ferredoxins are able to cover a wide range of redox potentials (−700 to −200 mV); however, the mechanisms underlying the factors which control the redox potential are still enigmatic. Here, we determined the neutron structure of ferredoxin from Bacillus thermoproteolyticus , and experimentally revealed the exact hydrogen-bonding network involving the [4Fe-4S] cluster. The density functional theory calculations based on the hydrogen-bonding network revealed that protonation states of the sidechain of Asp64 close to the [4Fe-4S] cluster critically affected the stability of the reduced state in the cluster. These findings provide the first identification of the intrinsic control factor of redox potential for the [4Fe-4S] cluster in low-potential ferredoxins.

### Competing Interest Statement

The authors have declared no competing interest.

Protonation/deprotonation-driven switch for the redox stability of low-potential [4Fe-4S] ferredoxin

저전위-페레독신의-산화환원-안정성을-제어하는-양성자화-탈양성자화-스위치-메커니즘-규명


저전위 페레독신의 산화환원 안정성을 제어하는 양성자화/탈양성자화 스위치 메커니즘 규명
