The crystal structure of the iron‐free cytochrome <i>c</i> peroxidase and its implication for the enzymatic mechanism

Yonetani, Takashi; Skoglund, Ulf

doi:10.1016/0014-5793(94)00910-4

Cited by 3 publications

(2 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The molecular origin of these transitions, however, does not appear to correspond to the domain structure (Kresheck and Erman, 1988). ApoCCP can form crystals (Yonetani, 1967), and the structure of the iron-free protein has been solved (Su et al, 1994;Bhaskar and Poulos, 2005). IUPRED identifies the stretch (120-145) at the end of the Nterminal portion of domain I as prone to disorder.…”

Section: Horseradish Peroxidase and Cytochrome C Peroxidasementioning

confidence: 96%

Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins

Landfried

Vuletich

Pond

et al. 2007

Gene

View full text Add to dashboard Cite

The binding of a cofactor to a protein matrix often involves a reorganization of the polypeptide structure. b Hemoproteins provide multiple examples of this behavior. In this minireview, selected monomeric and single b heme proteins endowed with distinct topological properties are inspected for the extent of induced refolding upon heme binding. To complement the data reported in the literature, original results are presented on a two-on-two globin of cyanobacterial origin (Synechococcus sp. PCC 7002 GlbN) and on the heme-containing module of FixL, an oxygen-sensing protein with the mixed alpha/beta topology of PAS domains. GlbN had a stable apoprotein that was further stabilized and locally refolded by heme binding; in contrast, apoFixLH presented features of a molten globule. Sequence analyses (helicity, disorder, and polarity) and solvent accessibility calculations were performed to identify trends in the architecture of b hemoproteins. In several cases, the primary structure appeared biased toward a partially disordered binding pocket in the absence of the cofactor.

show abstract

Section: Horseradish Peroxidase and Cytochrome C Peroxidasementioning

confidence: 96%

Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins

Landfried

Vuletich

Pond

et al. 2007

Gene

View full text Add to dashboard Cite

show abstract

“…The corner-L unit occurs in endochitinase (120-160) [14], hexokinase (260-300) [15], transcription factor LEF-1 [16] and others. The L-corner unit is found, for example, in ribonuclease Rh (71-112) [17] and cytochrome c peroxidase (118-168) [18].…”

Section: Some Additional Remarks On the Commonly Occurring Folding Unitsmentioning

confidence: 99%

A structural tree for α‐helical proteins containing α‐α‐corners and its application to protein classification

Ефимов

1996

FEBS Letters

View full text Add to dashboard Cite

A structural tree for a-helical proteins and domains including a-a-corners has been constructed. The a--a-corner is taken as a root structure of the tree. The larger protein structures are obtained by stepwise addition of a-helices to the root a-acorner taking into account a restricted set of rules inferred from known principles of protein structure. The protein structures that can be obtained in this way are grouped into one structural class and those found in branches of the tree into subclasses.

show abstract

The 1.13-Å structure of iron-free cytochrome c peroxidase

Bhaskar

Poulos

2005

J Biol Inorg Chem

View full text Add to dashboard Cite

The iron-free cytochrome c peroxidase (CCP) crystal structure has been determined to 1.13 A and compared with the 1.2-A ferric-CCP structure. Quite unexpectedly, removal of the iron has no effect on porphyrin geometry and distortion, indicating that protein-porphyrin interactions and not iron coordination or formation of the axial His-Fe bond determines porphyrin conformation. However, there are changes in solvent structure in the distal pocket, which lead to changes in the distal His52 acid-base catalyst. The observed ability of His52 to move in response to small changes in solvent structure is very likely important for its role as a catalyst in assisting in the heterolytic fission of the peroxide O-O bond.

show abstract

The crystal structure of the iron‐free cytochrome c peroxidase and its implication for the enzymatic mechanism

Cited by 3 publications

References 35 publications

Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins

Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins

A structural tree for α‐helical proteins containing α‐α‐corners and its application to protein classification

The 1.13-Å structure of iron-free cytochrome c peroxidase

Contact Info

Product

Resources

About