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Native Cu(A) redox sites are largely resilient to pH variations within a physiological range
Damián Alvarez-Paggi1, Luciano A Abriata, Daniel H Murgida
1INQUIMAE-CONICET and Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria Pab. 2, C1428EHA Buenos Aires, Argentina.
Engineered CuA centers undergo histidine protonation at physiological pH, unlike native CuA. This suggests native CuA may not regulate proton-coupled electron transfer via histidine protonation.
Area of Science:
- Biochemistry
- Bioinorganic Chemistry
- Spectroscopy
Background:
- Engineered CuA centers previously showed histidine protonation and dissociation at physiological pH.
- This suggested a role in regulating proton-coupled electron transfer in cytochrome c oxidases.
- The behavior of native CuA at physiological pH remained unclear.
Purpose of the Study:
- To investigate the protonation state of histidine ligands in native CuA at physiologically relevant pH.
- To determine if pH changes affect the spectroscopic and redox properties of the native CuA metal site.
Main Methods:
- Spectroscopic analysis of native CuA.
- Redox property measurements.
- pH-dependent studies.
Main Results:
- Native CuA does not exhibit histidine protonation at physiological pH.
- No significant changes in spectroscopic properties were observed at low pH.
- No significant changes in redox properties were observed at low pH.
Conclusions:
- The previously observed histidine protonation in engineered CuA does not occur in the native form.
- Native CuA's spectroscopic and redox properties are stable across a range of pH values.
- This challenges the proposed role of histidine protonation in regulating native CuA function in vivo.
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