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Daniel H. Murgida

Researcher at Facultad de Ciencias Exactas y Naturales

Publications -  133
Citations -  4535

Daniel H. Murgida is an academic researcher from Facultad de Ciencias Exactas y Naturales. The author has contributed to research in topics: Electron transfer & Cytochrome c. The author has an hindex of 37, co-authored 127 publications receiving 4125 citations. Previous affiliations of Daniel H. Murgida include University of the Republic & National Scientific and Technical Research Council.

Papers
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Electron-transfer processes of cytochrome C at interfaces. New insights by surface-enhanced resonance Raman spectroscopy.

TL;DR: It is shown that physiologically relevant electric field strengths can effectively modulate the electron-transfer dynamics and induce conformational transitions in heme protein cytochrome c.
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Mutational Analysis of Deinococcus radiodurans Bacteriophytochrome Reveals Key Amino Acids Necessary for the Photochromicity and Proton Exchange Cycle of Phytochromes

TL;DR: Using structurally guided site-directed mutagenesis combined with several spectroscopic methods, the roles of conserved amino acids within the bilin-binding domain of Deinococcus radiodurans bacteriophytochrome with respect to chromophore ligation and Pr/Pfr photoconversion are examined.
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Multifunctional Cytochrome c: Learning New Tricks from an Old Dog.

TL;DR: Current knowledge and recent advances in understanding the different structural, dynamic, and thermodynamic factors that regulate the primary electron transfer function, as well as alternative functions and conformations of cyt c are summarized.
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Light-induced proton release of phytochrome is coupled to the transient deprotonation of the tetrapyrrole chromophore

TL;DR: The coupling of transient chromophore deprotonation and proton release, which is likely to be an essential element in the Pr → Pfr photocon-version mechanism of phytochromes in general, may play a crucial role for the structural changes in the final step of the Pfr formation that switch between the active and the inactive state of the photoreceptor.