Zinc: Multidimensional Effects on Living Organisms
Biomedicines, 2021 Zinc is a redox-inert trace element that is second only to iron in abundance in biological systems. In cells, zinc is typically buffered and bound to metalloproteins, but it may also exist in a labile or chelatable (free ion) form.
Math P. Cuajungco +2 more
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Electron Flow through Metalloproteins [PDF]
Chemical Reviews, 2010 Electron transfers in photosynthesis and respiration commonly occur between metal-containing cofactors that are separated by large molecular distances. Understanding the underlying physics and chemistry of these biological electron transfer processes is the goal of much of the work in our laboratories.
Gray, Harry B., Winkler, Jay R.
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The Stereochemical Basis of the Genetic Code and the (Mostly) Autotrophic Origin of Life
Life, 2014 Spark-tube experiments and analysis of meteorite contents have led to the widespread notion that abiotic organic molecules were the first life components.
Juan C. Fontecilla-Camps
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Dihydropyrimidine-thiones and clioquinol synergize to target beta-amyloid cellular pathologies through a metal-dependent mechanism [PDF]
, 2017 The lack of therapies for neurodegenerative diseases arises from our incomplete understanding of their underlying cellular toxicities and the limited number of predictive model systems.
Barrasa, M. Inmaculada +9 more
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How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation [PDF]
, 2006 During the process of biological nitrogen fixation, the enzyme nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein;
Howard, James B., Rees, Douglas C.
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Electrochemical titrations and reaction time courses monitored in situ by magnetic circular dichroism spectroscopy [PDF]
, 2011 Magnetic circular dichroism (MCD) spectra, at ultraviolet–visible or near-infrared wavelengths (185–2000 nm), contain the same transitions observed in conventional absorbance spectroscopy, but their bisignate nature and more stringent selection rules ...
Abramson +52 more
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Towards the spatial resolution of metalloprotein charge states by detailed modeling of XFEL crystallographic diffraction. [PDF]
, 2020 Oxidation states of individual metal atoms within a metalloprotein can be assigned by examining X-ray absorption edges, which shift to higher energy for progressively more positive valence numbers.
Holton, James M +3 more
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Reactions of HNO with Metal Porphyrins: Underscoring the Biological Relevance of HNO [PDF]
, 2014 Azanone (1 HNO, nitroxyl) shows interesting yet poorly understood chemical and biological effects. HNO has some overlapping properties with nitric oxide (NO), sharing its biological reactivity toward heme proteins, thiols, and oxygen.
Bikiel, Damian Ezequiel +4 more
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Crystal structures of the NO sensor NsrR reveal how its iron-sulfur cluster modulates DNA binding
Nature Communications, 2017 NsrR is a bacterial transcriptional regulator that acts as a nitric oxide (NO) sensor. Here, the authors present the crystal structure of NsrR, which reveals an unusual Fe-S cluster coordination and explains how NO exposure leads to the degradation of ...
Anne Volbeda +7 more
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Structure and Dynamics of Metalloproteins in Live Cells [PDF]
, 2008 X-ray absorption spectroscopy (XAS) has emerged as one of the premier tools for investigating the structure and dynamic properties of metals in cells and in metal containing biomolecules. Utilizing the high flux and broad energy range of X-rays supplied
Cook, Jeremy D. +2 more
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