Conversion of an Electron-Transfer Protein into an Oxygen Binding Protein:  The Axial Cytochrome b5 Mutant with an Unusually High O2 Affinity

Ihara, Masaki; Shintaku, Masato; Takahashi, Satoshi; Ishimori, Koichiro; Morishima, Isao

doi:10.1021/ja002914r

Cited by 6 publications

(3 citation statements)

References 19 publications

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“…Moreover, by double mutation (Phe35Val/His39Leu), cyt b 5 can be converted from an electron-transfer protein into an oxygen carrier with an O 2 -binding affinity about 800 times higher than that of WT Mb. [7] Cyt b 562 is a periplasmic hemoprotein from Escherichia coli (E. coli) that belongs to a class of cytochromes sharing a common 4-a-helical fold. [2b, 8] With the exception of cyt b 562 , which binds heme noncovalently, all members of this class of cytochromes covalently bind their heme groups.…”

Section: Modification Of the Heme-binding Active Sitementioning

confidence: 99%

Rational Heme Protein Design: All Roads Lead to Rome

Lin

Sawyer

Wang

2013

Chemistry An Asian Journal

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Heme proteins are among the most abundant and important metalloproteins, exerting diverse biological functions including oxygen transport, small molecule sensing, selective CH bond activation, nitrite reduction, and electron transfer. Rational heme protein designs focus on the modification of the heme‐binding active site and the heme group, protein hybridization and domain swapping, and de novo design. These strategies not only provide us with unique advantages for illustrating the structure–property–reactivity–function (SPRF) relationship of heme proteins in nature but also endow us with the ability to create novel biocatalysts and biosensors.

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Section: Modification Of the Heme-binding Active Sitementioning

confidence: 99%

Rational Heme Protein Design: All Roads Lead to Rome

Lin

Sawyer

Wang

2013

Chemistry An Asian Journal

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“…Thus, the chemistry of the residue at position 39 exerts a key influence on the catalytic activity of the protein. Moreover, by double mutation (Phe35Val/His39Leu), cyt b 5 can be converted from an electron‐transfer protein into an oxygen carrier with an O 2 ‐binding affinity about 800 times higher than that of WT Mb 7…”

Section: Introductionmentioning

confidence: 99%

Operando Attenuated Total Reflectance FTIR Spectroscopy: Studies on the Different Selectivity Observed in Benzyl Alcohol Oxidation

et al. 2015

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Au, Pd, and AuPd supported on TiO2 were prepared by a sol immobilization route. Operando attenuated total reflectance (ATR) IR spectroscopy and catalytic batch reactor experiments were performed in parallel to elucidate the different catalytic performance of the catalysts in the liquid‐phase oxidation of benzyl alcohol. Pd/TiO2 exhibited a higher activity than AuPd/TiO2 and Au/TiO2, but the modification of Pd with Au demonstrated a significant stability enhancement. ATR‐IR spectroscopy evidenced that the presence of Au facilitates the desorption of byproducts, which thus reduces the extent of deactivation of the active sites caused by the irreversible adsorption of benzoate species. Although benzaldehyde was the main product in both catalysts, the nature of the byproducts differs. Pd/TiO2 favored the deoxygenation of benzyl alcohol to produce toluene as the main byproduct. Conversely, AuPd/TiO2 promoted the transformation of benzaldehyde to benzoic acid.

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“…Later on, Rivera and co-workers constructed other axial mutants of Cyt b5, such as H39V, H63M, and H63V Cyt b5, and found that these mutants perform an efficient oxidation of the heme [27,28]. Ihara et al also engineered a double mutant of Cyt b5 (F35V/H39L) by removing the axial ligand and fine-tuning the hydrophobic interactions in the heme pocket, and the double mutant exhibited an O2 binding affinity ~800 times higher than that of Mb, a native O2 carrier [29]. On the other hand, Huang and co-workers showed that when the axial His39 of Cyt b5 was replaced with hydrophilic residues such as Ser or Gln, the redesigned H39S and H39Q Cyt b5 variants exhibited peroxidase-like oxidation of guaiacol 193 and 113 times higher, respectively, than that of wild-type (WT) Cyt b5 [30].…”

Section: Redesign Of the Heme Pocketmentioning

confidence: 99%

Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions

Hirota

Lin

2017

J Biol Inorg Chem

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Noncovalent weak interactions [hydrophobic interaction and hydrogen (H)-bond] play crucial roles in controlling the functions of biomolecules, and thus have been used to design artificial metalloproteins/metalloenzymes during the past few decades. In this review, we focus on the recent progresses in protein design by tuning the noncovalent interactions, including hydrophobic and H-bonding interactions. The topics include redesign and reuse of the heme pocket and other protein scaffolds, design of the heme protein interface, and de novo design of metalloproteins. The informations not only give insights into the metalloenzyme reaction mechanisms but also provide new reactions for future applications.

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Conversion of an Electron-Transfer Protein into an Oxygen Binding Protein: The Axial Cytochrome b₅ Mutant with an Unusually High O₂ Affinity

Cited by 6 publications

References 19 publications

Rational Heme Protein Design: All Roads Lead to Rome

Rational Heme Protein Design: All Roads Lead to Rome

Operando Attenuated Total Reflectance FTIR Spectroscopy: Studies on the Different Selectivity Observed in Benzyl Alcohol Oxidation

Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions

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