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Probing the non‐native states of Cytochrome c with resonance Raman spectroscopy: A tool for investigating the structure–function relationship.
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- Journal of Raman Spectroscopy, 2018, v. 49, n. 6, p. 1041, doi. 10.1002/jrs.5315
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The influence of pH and anions on the adsorption mechanism of rifampicin on silver colloids.
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- Journal of Raman Spectroscopy, 2007, v. 38, n. 7, p. 859, doi. 10.1002/jrs.1727
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- Article
Surface-enhanced resonance Raman spectroscopy of rifamycins on silver nanoparticles: insight into their adsorption mechanisms.
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- Journal of Raman Spectroscopy, 2006, v. 37, n. 9, p. 900, doi. 10.1002/jrs.1519
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- Article
Spectroscopic and kinetic properties of the horseradish peroxidase mutant T171S.
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- FEBS Journal, 2005, v. 272, n. 21, p. 5514, doi. 10.1111/j.1742-4658.2005.04943.x
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- Article
An unusual temperature dependence of the EPR parameters of copper(II) and oxovanadium(IV) bis(acetylacetonate) complexes.
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- Magnetic Resonance in Chemistry, 1999, v. 37, n. 8, p. 538, doi. 10.1002/(SICI)1097-458X(199908)37:8<538::AID-MRC498>3.0.CO;2-0
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- Article
Pichia pastoris Fep1 is a [2Fe-2S] protein with a Zn finger that displays an unusual oxygen-dependent role in cluster binding.
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- Scientific Reports, 2016, p. 31872, doi. 10.1038/srep31872
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- Article
Oxygen-Linked S-Nitrosation in Fish Myoglobins: A Cysteine-Specific Tertiary Allosteric Effect.
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- PLoS ONE, 2014, v. 9, n. 5, p. 1, doi. 10.1371/journal.pone.0097012
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- Article
The Role of CyaY in Iron Sulfur Cluster Assembly on the E. coli IscU Scaffold Protein.
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- PLoS ONE, 2011, v. 6, n. 7, p. 1, doi. 10.1371/journal.pone.0021992
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- Article
Anion concentration modulates the conformation and stability of the molten globule of cytochrome c.
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- Journal of Biological Inorganic Chemistry (JBIC), 2003, v. 8, n. 6, p. 663, doi. 10.1007/s00775-003-0462-7
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From chlorite dismutase towards HemQ - the role of the proximal H-bonding network in haeme binding.
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- Bioscience Reports, 2016, v. 36, n. 2, p. 1, doi. 10.1042/BSR20150330
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- Article
Resonance Raman and electronic absorption spectra of horseradish peroxidase isozyme A2: evidence for a quantum-mixed spin species.
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- Journal of Raman Spectroscopy, 1998, v. 29, n. 10/11, p. 933, doi. 10.1002/(SICI)1097-4555(199810/11)29:10/11<933::AID-JRS319>3.0.CO;2-P
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- Article
Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125.
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- FEBS Journal, 2015, v. 282, n. 15, p. 2948, doi. 10.1111/febs.13335
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- Article
Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins.
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- Biopolymers, 2009, v. 91, n. 12, p. 1117, doi. 10.1002/bip.21206
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Mutation of residues critical for benzohydroxamic acid binding to horseradish peroxidase isoenzyme C.
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- Biopolymers, 2001, v. 62, n. 5, p. 261, doi. 10.1002/bip.1021
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Ligand- and proton-linked conformational changes of the ferrous 2/2 hemoglobin of Pseudoalteromonas haloplanktis TAC125.
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- IUBMB Life, 2011, v. 63, n. 7, p. 566, doi. 10.1002/iub.492
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Occurrence and formation of endogenous histidine hexa-coordination in cold-adapted hemoglobins.
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- IUBMB Life, 2011, v. 63, n. 5, p. 295, doi. 10.1002/iub.446
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- Article
ATP specifically drives refolding of non-native conformations of cytochrome c.
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- Protein Science: A Publication of the Protein Society, 2005, v. 14, n. 4, p. 1049, doi. 10.1110/ps.041069405
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Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes.
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- Protein Science: A Publication of the Protein Society, 2004, v. 13, n. 10, p. 2766, doi. 10.1110/ps.04861504
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Structural determinants of ligand binding in truncated hemoglobins: Resonance Raman spectroscopy of the native states and their carbon monoxide and hydroxide complexes.
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- Biopolymers, 2018, v. 109, n. 10, p. N.PAG, doi. 10.1002/bip.23114
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Insights into the role of the histidines in the structure and stability of cytochrome c.
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- Journal of Biological Inorganic Chemistry (JBIC), 2006, v. 11, n. 1, p. 52, doi. 10.1007/s00775-005-0057-6
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The 40s Ω-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c.
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- Journal of Biological Inorganic Chemistry (JBIC), 2004, v. 9, n. 8, p. 997, doi. 10.1007/s00775-004-0601-9
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Nanohybrid Assemblies of Porphyrin and Au10 Cluster Nanoparticles.
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- Nanomaterials (2079-4991), 2019, v. 9, n. 7, p. 1026, doi. 10.3390/nano9071026
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