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Last update 08 May 2025

cyt bc1

Last update 08 May 2025

Basic Info

Synonyms

coenzyme Q : cytochrome c – oxidoreductase, complex III, dihydrocoenzyme Q-cytochrome c reductase

+ [4]

Introduction

Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.

Drugs associated with cyt bc1

HIF-143

Target

cyt bc1

Mechanism

cyt bc1 inhibitors

Active Org.-

Originator Org.

Oscotec, Inc.

Active Indication-

Inactive Indication

Pancreatic Cancer

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

ELQ-400

Target

cyt bc1

Mechanism

cyt bc1 inhibitors

Active Org.-

Originator Org.

Oregon Health & Science University

Active Indication-

Inactive Indication

Malaria

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with cyt bc1

100 Translational Medicine associated with cyt bc1

0 Patents (Medical) associated with cyt bc1

1,586

Literatures (Medical) associated with cyt bc1

01 Dec 2025·Histochemistry and Cell Biology

Mechanisms of S-phase arrest and mitochondrial dysfunction in complex III by DHODH inhibitors in tumorigenic TNBC cells

Article

Author: Nor Rashid, Nurshamimi ; Shahhiran, Muhammad Aiman Akmal ; Abdul-Rahman, Puteri Shafinaz ; Othman, Shatrah ; Abdul Kadir, Mohamad Fairus

Dihydroorotate dehydrogenase (DHODH) inhibitors have recently gained increasing research interest owing to their potential for treating breast cancers. We explored their effects in different breast cancer subtypes, focusing on mitochondrial dysfunction. The sensitivity of different subtypes to the inhibitors was investigated with respect to DHODH expression, tumorigenic, and receptor status. Analysis of respiratory complexes, cell cycle, reactive oxygen species (ROS), and cell differentiation were performed. Four cell lines with different receptor status were included, namely MCF-7, MDAMB-231, SKBR-3, and MCF-10A. We showed that MCF-7 and MDAMB-231 cells of the subtypes (ER⁺/PR⁺/HER2^-) and (ER^-/PR^-/HER2^-), respectively, were responsive to brequinar. Brequinar (BQR) caused cell cycle arrest in the S-phase in sensitive subtypes of breast cells but induced cell differentiation only in poorly differentiated breast cells. All cell subtypes showed increased generation of ROS, both intracellular and mitochondrial ROS with a greater increase seen in mitochondrial ROS in response to DHODH inhibitor, subsequently contributing to mitochondrial dysfunction. BQR also disrupts the function of complex III in ER⁺/PR⁺ and triple negative breast cancer (TNBC) subtypes. Collectively, we have found that MDAMB-231 TNBC cell was the most affected by DHODH inhibition in terms of sensitivity, cell cycle arrest, induction of cell differentiation, production of ROS, and mitochondrial complexes disruption. In conclusion, these findings suggest that DHODH inhibitors can potentially become a valuable targeted therapy for TNBC subtype and further consolidates its therapeutic potential as part of the combinatorial therapy against this resilient breast cancer subtype.

01 Jun 2025·Journal of Hazardous Materials

Mechanistic insights into the response of oxygen reducing biocathode to Ni2 +: Microbial activity and electron transfer behavior

Article

Author: Tang, Xinyue ; Zhou, Xiaoyu ; Xue, Jianliang ; Dong, Xing ; Qiao, Yanlu ; Shi, Ke ; Jiang, Qing ; Song, Xiangru ; Feng, Yujie ; Cheng, Dongle

Heavy metals affect the electrochemical activity of microorganisms in bioelectrochemical systems. However, effects of heavy metals on microbial viability and extracellular electron transfer of oxygen reducing biocathodes remains elusive. This study indicated that the impact of Ni²⁺ shock was concentration-dependent. At 1 mg L^-1, current density and electrochemical performance improved, with the highest live cell proportion (73.2 %). Conversely, higher concentrations (10 and 100 mg L^-1) showed negative effects, with increasing cell death and biocathode damage. Functional groups (i.e. carbonyl CO, N-H, C-H, and C-O-C), and proteins, humic acid of LB-EPS were confirmed to bind with Ni²⁺, preventing the penetration into cells. Increased Ni²⁺ levels intensified interactions with biofilm functional groups, reducing direct electron transfer between oxygen reducing biofilm and cathode. Ni²⁺ shock altered the structure and microbial richness of the cathode biofilms, decreasing electron transfer gene abundance (e.g., nikA, sodN) and increasing heavy metal resistance genes (e.g., czcB, TC.HME) at higher Ni²⁺ concentrations. Molecular docking showed Ni²⁺ interacted variably with electron transfer enzymes, strongly binding to succinate dehydrogenase and cytochrome bc1 complex, affecting enzyme activity and metabolism. This research enhanced understanding of biofilm response to Ni²⁺ shock and provided insights for improving performance in heavy metal wastewater.

01 Jun 2025·Water Research

Synthetic microbial community maintains the functional stability of aerobic denitrification under environmental disturbances: Insight into the mechanism of interspecific division of labor

Article

Author: Xu, Ting ; Yun, Hui ; Peng, Liang ; Wang, Wenxue ; He, Yue ; Zhang, Wenjie ; Li, Xiangkai

Understanding how synthetic microbial community (SMC) respond to environmental disturbances is the key to realizing SMC engineering applications. Here, dibutyl phthalate (DBP) and levofloxacin (LOFX) were used as environmental disturbances to study their effects on the aerobic denitrification functional stability of SMC composed of Pseudomonas aeruginosa N2 (PA), Acinetobacter baumannii N1(AC) and Aeromonas hydrophila (AH). The results showed that aerobic denitrification efficiency could be maintained at about 93 % under DBP or LOFX disturbance, and interspecific communication was mainly carried out through N-butyryl-L-homoserine lactone (C₄-HSL) and N-(3-oxododecanoyl)-L-homoserine lactone (3OC₁₂-HSL), correspondingly. DBP and LOFX induced the acceleration of tricarboxylic acid (TCA) cycle, which facilitated the energy flux and extracellular polymeric substances (EPS) production, thereby allowing SMC to adapt to disturbances. Under DBP disturbance, DBP stimulated phenazine-1-carboxylic acid production to accelerate electron transfer from the quinone pool to complex III, resulting in an increase in electron transfer activity. Up-regulation of complex I, complex III and heme synthesis genes under LOFX disturbance led to enhanced denitrification enzymes expression and electron transfer efficiency. SMC re-regulated different metabolic pathways to build metabolic networks to maintain normal metabolic activity under different disturbances. Overall, SMC maintained functional stability through the labor division in modulation of interspecific communication, formation of defensive barriers, promotion of energy flux, directional transfer of electron flux, and reconstruction of metabolic networks. DBP stimulated AH and PA to occupy functional dominance, while LOFX induced AC and PA to play a major role. The understanding of the stability mechanism under different environmental disturbances provides valuable guidance for stability maintenance and engineering applications of SMC.

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