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Article

Highly conserved residues Asp-197 and His-250 in Agp1 phytochrome control the proton affinity of the chromophore and Pfr formation.

The Journal of biological chemistry - 19 Jan 2007

von Stetten David, Seibeck Sven, Michael Norbert, Scheerer Patrick, Mroginski Maria Andrea, Murgida Daniel H, Krauss Norbert, Heyn Maarten P, Hildebrandt Peter, Borucki Berthold, Lamparter Tilman

Abstract excerpt

The mutants H250A and D197A of Agp1 phytochrome from Agrobacterium tumefaciens were prepared and investigated by different spectroscopic and biochemical methods. Asp-197 and His-250 are highly conserved amino acids and are part of the hydrogen-bonding network that involves the chromophore. Both substitutions cause a destabilization of the protonated chromophore in the Pr state as revealed by resonance Raman and...

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PMID: 17121858
DOI: 10.1074/jbc.M608878200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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