The role of the heme propionates in heme biochemistry

Guallar, Vı́ctor; Olsen, Brett N.

doi:10.1016/j.jinorgbio.2006.01.019

Cited by 60 publications

(50 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In such a model, where the haem group and the aspartic acid are both treated at the quantum level of theory, electrons can flow freely between these two moieties. The results indicate a oneelectron transfer from the duet propionate-aspartic to the metal centre (Guallar & Olsen 2006). Thus, the third unpaired electron moves, respectively delocalizes, all the way to Asp297.…”

Section: Short Electron Transfer Electron Delocalization In Compound Imentioning

confidence: 89%

“…Thus, the third unpaired electron partially delocalizes into the propionate groups. These results generated quite a controversy and produced several additional studies by us and other groups (Schoneboom et al 2004;Altun et al 2006Altun et al , 2007Guallar & Olsen 2006;Zheng et al 2006;Zurek et al 2006).…”

Section: Short Electron Transfer Electron Delocalization In Compound Imentioning

confidence: 99%

See 1 more Smart Citation

Mapping protein electron transfer pathways with QM/MM methods

Guallar

Wallrapp

2008

J. R. Soc. Interface.

Self Cite

View full text Add to dashboard Cite

Mixed quantum mechanics/molecular mechanics (QM/MM) methods offer a valuable computational tool for understanding the electron transfer pathway in protein-substrate interactions and protein-protein complexes. These hybrid methods are capable of solving the Schrödinger equation on a small subset of the protein, the quantum region, describing its electronic structure under the polarization effects of the remainder of the protein. By selectively turning on and off different residues in the quantum region, we are able to obtain the electron pathway for short-and large-range interactions. Here, we summarize recent studies involving the protein-substrate interaction in cytochrome P450 camphor, ascorbate peroxidase and cytochrome c peroxidase, and propose a novel approach for the long-range protein-protein electron transfer. The results on ascorbate peroxidase and cytochrome c peroxidase reveal the importance of the propionate groups in the electron transfer pathway. The long-range protein-protein electron transfer has been studied on the cytochrome c peroxidase-cytochrome c complex. The results indicate the importance of Phe82 and Cys81 on cytochrome c, and of Asn196, Ala194, Ala176 and His175 on cytochrome c peroxidase.

show abstract

Section: Short Electron Transfer Electron Delocalization In Compound Imentioning

confidence: 89%

Section: Short Electron Transfer Electron Delocalization In Compound Imentioning

confidence: 99%

Mapping protein electron transfer pathways with QM/MM methods

Guallar

Wallrapp

2008

J. R. Soc. Interface.

Self Cite

View full text Add to dashboard Cite

show abstract

“…In previous studies, motivated by the experimental work of Barrows et al [79], we could transfer almost 0.4 electron units from the porphyrin moiety into the tryptophan by altering the electrostatic screening of the APX's propionates [80]. Further analysis of the role of the propionates in peroxidases indicated that this carboxylic group could play an active role in the transport of electrons in/out the heme group.…”

Section: Compound Imentioning

confidence: 95%

QM/MM methods: Looking inside heme proteins biochemisty

Guallar

Wallrapp

2010

Biophysical Chemistry

Self Cite

View full text Add to dashboard Cite

“…Thus, R329 may not always be necessary for the reaction. Heme propionate also plays an important role in the catalytic cycle [89]. In the case of TyrA, it has been proposed that the propionate on pyrrole IV rotates into a less common rotamer to accommodate a hydrogen bonding network between the propionic carboxylate, R206, R242, a water molecule , and the propionate of pyrrole III [41].…”

mentioning

confidence: 99%

DyP-type peroxidases comprise a novel heme peroxidase family

Sugano

2008

Cell. Mol. Life Sci.

226

261

View full text Add to dashboard Cite

Dye-decolorizing peroxidase (DyP) is produced by a basidiomycete (Thanatephorus cucumeris Dec 1) and is a member of a novel heme peroxidase family (DyP-type peroxidase family) that appears to be distinct from general peroxidases. Thus far, 80 putative members of this family have been registered in the PeroxiBase database (http://peroxibase.isbsib.ch/) and more than 400 homologous proteins have been detected via PSI-BLAST search. Although few studies have characterized the function and structure of these proteins, they appear to be bifunctional enzymes with hydrolase or oxygenase, as well as typical peroxidase activities. DyP-type peroxidase family suggests an ancient root compared with other general peroxidases because of their widespread distribution in the living world. In this review, firstly, an outline of the characteristics of DyP from T. cucumeris is presented and then interesting characteristics of the DyP-type peroxidase family are discussed.

show abstract

The role of the heme propionates in heme biochemistry

Cited by 60 publications

References 46 publications

Mapping protein electron transfer pathways with QM/MM methods

Mapping protein electron transfer pathways with QM/MM methods

QM/MM methods: Looking inside heme proteins biochemisty

DyP-type peroxidases comprise a novel heme peroxidase family

Contact Info

Product

Resources

About