Related Experiment Video
Updated: Aug 25, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
Why do c-type cytochromes exist? Reprise
1Department of Biochemistry, University of Bristol, U.K.
Insights
Covalent links in c-type haem likely evolved to prevent haem loss. This understanding aids in analyzing electron transfer chains, with exceptions in some bacteria.
Area of Science:
- Biochemistry
- Microbiology
- Cell Biology
Background:
- The function of c-type haem and its covalent linkage is crucial in biological electron transfer.
- Previous research suggested covalent haem attachment prevents loss into the external environment.
- Understanding haem's localization is key to deciphering complex biological pathways.
Purpose of the Study:
- To re-evaluate the hypothesis that covalent links in c-type haem prevent extracellular loss.
- To explore the implications of this hypothesis across diverse organisms and cellular compartments.
- To provide a framework for interpreting electron transfer chains by predicting cytochrome localization.
Main Methods:
- Comparative analysis of c-type haem distribution in various organisms (bacteria, eukaryotes).
- Review of existing literature on haem attachment mechanisms and prosthetic group stability.
- Examination of electron transfer pathways and the role of cytochromes.
Main Results:
- The hypothesis is supported by the distribution of c-type haem in Gram-negative and Gram-positive bacteria, cyanobacteria, and eukaryotes.
- C-type cytochromes are generally absent from the cytoplasm, with sulphate-reducing bacteria as a notable exception.
- Non-covalently bound haem is susceptible to loss, unlike covalently attached haem.
Conclusions:
- The covalent linkage of c-type haem serves as a critical adaptation to prevent its loss.
- This principle aids in predicting the absence of cytoplasmic c-type cytochromes, simplifying the study of electron transport chains.
- Analogies with other prosthetic groups like flavins and pyrroloquinoline quinone highlight conserved strategies in biological systems.
Abstract:
An earlier paper (Wood, P.M. (1983) FEBS Lett. 164, 223-226) proposed that the covalent links that characterize c-type haem originated in order to prevent the haem being lost into the external medium. This is discussed in relation to Gram-negative and Gram-positive bacteria, cyanobacterial thylakoids and eukaryotes. The practical application is for unravelling complex electron transfer chains: c-type cytochromes may be assumed to be absent from the cytoplasm. Sulphate reducing bacteria provide the only confirmed exception to this rule. Examples of non-covalent haem at risk of being lost are considered. Analogies are drawn with flavin and pyrroloquinoline quinone as prosthetic groups.
Related Concept Videos
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
The Supercomplexes in the Crista Membrane
Thermal and Photochemical Electrocyclic Reactions: Overview
Electron Transport Chain: Complex III and IV
Pericyclic Reactions: Introduction
Pericyclic reactions can be classified into three categories: electrocyclic reactions, cycloaddition reactions, and sigmatropic rearrangements. Electrocyclic reactions and sigmatropic rearrangements are...

