Structural and Biochemical Studies on Novel Bacterial Heme Proteins

Abstract

Heme an iron-porphyrin prosthetic group is essential for multiple biochemical functions including respiration, electron transfer, oxidative stress mitigation, and energy metabolism. In bacteria, hemoproteins support diverse physiological processes and act as key virulence determinants in pathogenic interactions with hosts. Bacteria have evolved sophisticated systems for acquiring, trafficking, degrading, and synthesizing heme, notably under iron-limited conditions imposed by host nutritional immunity. Recent structural and biochemical studies reveal alternative heme biosynthesis pathways, non-canonical degradation systems, intricate regulatory networks (including Fur-dependent and post-transcriptional controls), and emerging roles of heme in cell signaling and environmental sensing. This review synthesizes current understanding of bacterial heme structure, function, uptake and trafficking, degradation and biosynthesis, regulation, and potential antimicrobial targets, with an emphasis on advances from 2022 to 2025.