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#bacterial defense

2 public questions tagged with this topic.

Which enzyme is crucial for breaking down hydrogen peroxide in aerobic bacteria?

Aerobic respiration inevitably leaks electrons to dioxygen generating superoxide and hydrogen peroxide. H2O2 is particularly hazardous because ferrous iron drives Fenton reaction producing hydroxyl radical that nicks DNA phosphodiester backbone, carbonylates proteins, and peroxidizes lipids. Aerobes counter with catalase, extraordinarily efficient heme tetramer with kcat approaching ten million per second, diffusion limited perfect enzyme. Active site ferriprotoporphyrin IX cycles between ferric resting state and Compound I oxoferryl radical after binding first H2O2, then reduced by second H2O

Ref: Madigan et al., Brock Biology of Microorganisms, 16th ed., Chapter 6: Oxidative stress - Catalase mechanism.

The primary function of glutathione in bacterial stress response is:

Glutathione is a low-molecular-weight tripeptide gamma-glutamyl-cysteinyl-glycine present at millimolar concentrations up to 10 mM in many Gram-negative bacteria such as Escherichia coli and few Gram-positives that synthesize it via GshA and GshB. Reduced form GSH serves as major thiol buffer and electron donor protecting against reactive oxygen species generated continuously by endogenous respiratory electron transport and by host immune oxidative burst involving NADPH oxidase-dependent production of superoxide during phagocytosis. It directly scavenges superoxide anion, hydroxyl radical and

Ref: Prescott's Microbiology, 11th ed., Chapter 7: Glutathione and Oxidative Stress Protection in Bacteria.