Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: A comparative study

Viola, Franca; Aime, Silvio; Coletta, Massimo; Desideri, Alessandro; Fasano, Mauro; Paoletti, Silvia; Tarricone, C.; Ascenzi, Paolo

doi:10.1016/0162-0134(95)00155-7

Cited by 42 publications

(35 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The spectra of cytochrome c (1.48 M) encapsulated inside the lipid vesicle matched with that in aqueous buffer solution indicating that the protein is solubilized in the aqueous core of the vesicle (11,12). Addition of sodium azide (10 mM) to an aqueous buffer solution of cytochrome c forms the azide complex of the protein characterized by a distinct red shift in the Soret band to 410 nm.…”

Section: Effect Of H 2 O 2 and Ko 2 On The Release Of Cytochrome C Frmentioning

confidence: 88%

“…The extruded mixture was then passed through a Superdex-75 column to remove any free protein. Cytochrome c encapsulated inside vesicles were characterized by absorption spectra (11,12).…”

Section: Preparation Of Lipid-encapsulated Cytochrome C Solutionmentioning

confidence: 99%

“…The UV-visible spectra of cytochrome c in aqueous buffer at pH 7 shows the Soret band at 408 nm, and the visible band at 527 nm with a shoulder at 550 nm (11,12). The spectra of cytochrome c (1.48 M) encapsulated inside the lipid vesicle matched with that in aqueous buffer solution indicating that the protein is solubilized in the aqueous core of the vesicle (11,12).…”

Section: Effect Of H 2 O 2 and Ko 2 On The Release Of Cytochrome C Frmentioning

confidence: 99%

“…Addition of sodium azide (10 mM) to an aqueous buffer solution of cytochrome c forms the azide complex of the protein characterized by a distinct red shift in the Soret band to 410 nm. Figure 1 (graph a) gives the difference spectrum in the Soret region of the protein obtained on subtraction of the spectrum of the azide complex from that of the native protein, which shows distinct positive band at 397 nm and negative band at 414 nm corresponding the native protein and the azide complex respectively (11). Difference between the absorption spectra of the solution before and after addition of sodium azide given in Fig.…”

Section: Effect Of H 2 O 2 and Ko 2 On The Release Of Cytochrome C Frmentioning

confidence: 99%

“…Owing to the high positive surface charge, cytochrome c cannot come out to the cytosol from the inter membrane space of the mitochondrion under normal circumstances except during apoptosis (10,11). The mechanism of release of cytochrome c from the mitochondrion during apoptosis is yet to be understood.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Direct Observation of Release of Cytochrome c from Lipid-Encapsulated Protein by Peroxide and Superoxide: A Possible Mechanism for Drug-Induced Apoptosis

Das

Gupta

Mazumdar

2001

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

Section: Effect Of H 2 O 2 and Ko 2 On The Release Of Cytochrome C Frmentioning

confidence: 88%

“…The extruded mixture was then passed through a Superdex-75 column to remove any free protein. Cytochrome c encapsulated inside vesicles were characterized by absorption spectra (11,12).…”

Section: Preparation Of Lipid-encapsulated Cytochrome C Solutionmentioning

confidence: 99%

Section: Effect Of H 2 O 2 and Ko 2 On The Release Of Cytochrome C Frmentioning

confidence: 99%

Section: Effect Of H 2 O 2 and Ko 2 On The Release Of Cytochrome C Frmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Direct Observation of Release of Cytochrome c from Lipid-Encapsulated Protein by Peroxide and Superoxide: A Possible Mechanism for Drug-Induced Apoptosis

Das

Gupta

Mazumdar

2001

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

Long‐Range Electron Transfer through a Single‐walled Carbon Nanotube Sheet

et al. 2008

View full text Add to dashboard Cite

A flow reactor system is designed for the reduction of cytochrome c mediated by a sheet of single‐walled carbon nanotubes, as schematically illustrated in the figure. The reaction kinetics of the reduction of cytochrome c by an added reductant solution is monitored by optical absorption spectroscopy to elucidate the mechanism of long‐range electron transfer in this novel bio‐inspired reactor.

show abstract

Probing Bis‐Fe^IV MauG: Experimental Evidence for the Long‐Range Charge‐Resonance Model

2015

View full text Add to dashboard Cite

The biosynthesis of tryptophan tryptophylquinone, a protein-derived cofactor, involves a longrange reaction mediated by a bis-Fe(IV) intermediate of a di-heme enzyme, MauG. Recently, a unique charge-resonance (CR) phenomenon was discovered in this intermediate, and a biological, long-distance CR model was proposed. This model suggests that the chemical nature of the bisFe(IV) species is not as simple as it appears; rather, it is composed of a collection of resonance structures in a dynamic equilibrium. Here, we experimentally evaluated the proposed CR model by introducing small molecules to, and measuring the temperature dependence of, bis-Fe(IV) MauG. Spectroscopic evidence was presented to demonstrate that the selected compounds increase the decay rate of the bis-Fe(IV) species via disrupting the equilibrium of the resonance structures that constitutes the proposed CR model. The results support this new CR model and bring a fresh concept to the classical CR theory. Keywords charge resonance; electronic structure; heme proteins; high-valence iron; near-infrared Since its first documentation by Brocklehurst and Badgers in 1968, [1] charge-resonance (CR) phenomena have been actively researched by organic chemists. [2] In a typical CR event, one-electron oxidation of an aromatic compound generates a cation radical which spontaneously associates with its neutral parent molecule or another molecule of the cation radical to form non-covalent "sandwich-like" dimeric complexes. The former scenario stabilizes an odd number of spin/charge in a mixed-valence species, (Π) 2•+ , and is classified as Type I CR; the latter one stabilizes an even number of spin/charge in a di-cation diradical, (Π 2 •+ ), and is classified as Type II CR. [3] Notably, unique electronic absorption bands in the near-infrared (NIR) region arise from resonance stabilization of spin/charge in the CR complexes and are thereby termed as CR bands (see Figure S1 for an MO-diagram illustration). [4][5][6][7] CR complexes represent the simplest intermolecular units that carry delocalized spin/charge. Investigation of these phenomena may provide the chemical basisCorrespondence to: Aimin Liu, Feradical@gsu.edu. Supporting information for this article is given via a link at the end of the document. HHS Public AccessAuthor manuscript Author ManuscriptAuthor Manuscript Author ManuscriptAuthor Manuscript for electron transfer (ET), conductivity, and ferromagnetism in many organic materials and metalloporphyrin complexes.Like many classical chemical models adopted by nature, the utilization of CR in biological systems to transiently stabilize spin/charge was first suggested in a pair of chlorophyll molecules, known as the "special pair", in bacterial photosynthetic reaction centers. [8][9] Recently, a second example was revealed from a di-heme enzyme, MauG. [3] MauG is the terminal enzyme in the biogenesis pathway of a protein-derived cofactor, tryptophan tryptophylquinone (TTQ), [10] which is the catalytic center of methylamine dehydrogenase (MADH). [1...

show abstract

Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: A comparative study

Cited by 42 publications

References 44 publications

Direct Observation of Release of Cytochrome c from Lipid-Encapsulated Protein by Peroxide and Superoxide: A Possible Mechanism for Drug-Induced Apoptosis

Direct Observation of Release of Cytochrome c from Lipid-Encapsulated Protein by Peroxide and Superoxide: A Possible Mechanism for Drug-Induced Apoptosis

Long‐Range Electron Transfer through a Single‐walled Carbon Nanotube Sheet

Probing Bis‐Fe^IV MauG: Experimental Evidence for the Long‐Range Charge‐Resonance Model

Contact Info

Product

Resources

About

Azide, cyanide, fluoride, imidazole and pyridine binding to ferric and ferrous native horse heart cytochrome c and to its carboxymethylated derivative: A comparative study

Cited by 42 publications

References 44 publications

Direct Observation of Release of Cytochrome c from Lipid-Encapsulated Protein by Peroxide and Superoxide: A Possible Mechanism for Drug-Induced Apoptosis

Direct Observation of Release of Cytochrome c from Lipid-Encapsulated Protein by Peroxide and Superoxide: A Possible Mechanism for Drug-Induced Apoptosis

Long‐Range Electron Transfer through a Single‐walled Carbon Nanotube Sheet

Probing Bis‐FeIV MauG: Experimental Evidence for the Long‐Range Charge‐Resonance Model

Contact Info

Product

Resources

About

Probing Bis‐Fe^IV MauG: Experimental Evidence for the Long‐Range Charge‐Resonance Model