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19 Cards in this Set
- Front
- Back
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What can sulphur redox changes can fundamentally change the structure and or function of |
Small thiol molecules sometimes irreversible |
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Where is N.B present in DNA or protein |
Protein |
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What is N.B being present in useful for |
Useful for radio labelling experiments |
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What are sulphate reducers |
H2 or organic compounds as e- donors generally anaerobic |
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What are sulphur reducers |
Reduces S^0 to H2S |
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What are sulphur oxidisers |
Oxidise S^0, H2S, thiosulphate, thiocyanate |
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What is acquisition os sulphur for the synthesis of biological molecules |
Generally, inorganic —> cysteine |
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What can’t cysteine be used to make |
Other S- containing compounds |
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What are the two most important amino acids |
Cysteine and methionine |
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How do you make sure the right protein gets the right redox state in E. Coli |
Compartmentalisation Periplasm is oxidising, cytoplasm is reducing environment |
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What are the exceptions to compartmentalisation |
Anaerobes and Intracellular bacteria many not form S-Ss in proteins at all; some archaea form S-S bonds in cytoplasmic proteins |
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What is DsbAB |
Disulphide bond formation (co- or post- translational) |
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What he DsbCD wha |
Disulphide bond isomerization and chaperone activity |
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What happens to strains lacking dsbA or dsbB |
Defective in S-S formation in periplasmic proteins MalF-LacZ reporter fusion Alkaline phosphates Flgl flagellate motility LptD aka Imp, FtsN |
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What is dsbAB linked to |
Virulence in many bacterial pathogens Targeting S-S formation |
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What cytoplasmic proteins absolutely require reduced thinks for their activity |
Ribonucleotide reductase PAPS reductase Arsenate reductase |
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What is glutathione |
A key redox buffer, osmoprotectant, defence against toxic compounds |
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What are reactive oxygen specified and reactive nitrogen species produced by |
The host to kill bacteria |
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What must pathogens be able to sense what |
Stress and respond |
