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Yoshitaka Yoda

Researcher at Lawrence Berkeley National Laboratory

Publications -  7
Citations -  429

Yoshitaka Yoda is an academic researcher from Lawrence Berkeley National Laboratory. The author has contributed to research in topics: Nuclear resonance vibrational spectroscopy & Resonance. The author has an hindex of 6, co-authored 7 publications receiving 401 citations. Previous affiliations of Yoshitaka Yoda include Massachusetts Institute of Technology & Max Planck Society.

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Characterization of iron dinitrosyl species formed in the reaction of nitric oxide with a biological Rieske center.

TL;DR: It is demonstrated that NO reacts readily with a Rieske center in a protein and suggested that dinuclear RRE species, not mononuclear DNICs, may be the primary iron dinitrosyl species responsible for the pathological and physiological effects of nitric oxide in such systems in biology.
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Characterization of the Fe Site in Iron-Sulfur Cluster-Free Hydrogenase (Hmd) and of a Model Compound via Nuclear Resonance Vibrational Spectroscopy (NRVS)

TL;DR: (57)Fe nuclear resonance vibrational spectroscopy (NRVS) is used to study the iron site in the iron-sulfur cluster-free hydrogenase Hmd from the methanogenic archaeon Methanothermobacter marburgensis to provide further insight into the dynamics of the Fe site.
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How Nitrogenase Shakes – Initial Information about P-Cluster and FeMo-cofactor Normal Modes from Nuclear Resonance Vibrational Spectroscopy (NRVS)

TL;DR: This work has used the synchrotron technique of (57)Fe nuclear resonance vibrational spectroscopy (NRVS) to study the dynamics of the Fe-S clusters in nitrogenase, and presents the first spectroscopic information about the vibrational modes of the intact nitrogenase FeMo-cofactor and P-cluster.
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Normal mode analysis of Pyrococcus furiosus rubredoxin via nuclear resonance vibrational spectroscopy (NRVS) and resonance raman spectroscopy.

TL;DR: The results confirm the delocalization of the dynamic properties of the redox-active Fe site and demonstrate great promise for the observation and quantitative interpretation of the dynamical properties of Fe-S proteins.
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Extended X-ray absorption fine structure and nuclear resonance vibrational spectroscopy reveal that NifB-co, a FeMo-co precursor, comprises a 6Fe core with an interstitial light atom.

TL;DR: The results are consistent with the conclusion that the interstitial light atom is already present at an early stage in FeMo-co biosynthesis prior to the incorporation of Mo and R-homocitrate.