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Nicolas Caramello @ncaramel.bsky.social · 16/02/2026

I'm proud to present this first article from my PostDoc: We probed the different responses of metalloproteins (myoglobin, Mb and a copper-containing Nitrite Reductase, CuNIR) to reduction of their metal centres by X-rays at two temperatures (100K, 392K-RT) with UV-vis absorption and diffraction.

journals.iucr.org

Coupled on-line in crystallo UV–Vis absorption spectroscopy and X-ray crystallography to compare specific radiation damage in metal-containing proteins at room versus cryogenic temperature

We used on-line in crystallo UV–Vis absorption spectroscopy in conjunction with X-ray crystallography on beamline BM07-FIP2 at the ESRF to compare the structural effects of specific radiation damage o...

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Nicolas Caramello @ncaramel.bsky.social · 16/02/2026

We find that temperature is a defining factor in the response to X-ray-induced reduction of both Mb and CuNIR's metal centres. UV-vis spectroscopy identified different species of the haem iron induced by X-ray exposure in Mb (hexavalent ferrous at 100K vs pentavalent ferrous at RT).

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Nicolas Caramello @ncaramel.bsky.social · 16/02/2026

It also evidenced that temperature altered the electron-transfer kinetics between Type 1 copper (reduced by X-ray exposure) and Type 2 copper (active site of CuNIR). Diffraction confirmed that in both cases, this is a consequence of the increased rigidity of metal centre environments at 100K.

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