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Wright State University

1. Fisher, Kelli Nicole. Investigating the Undefined Role of Subunit IIIin Cytochrome c Oxidase Functioning Using Dicyclohexylcarbodiimide Chemical Modification; Insight Into Enzyme Structure and Molecular Mechanism.

Degree: MS, Biochemistry and Molecular Biology, 2014, Wright State University

In the cell metabolic cycle, cytochrome c oxidase (COX) is the final electron acceptor of the respiratory chain which reduces molecular oxygen into water. It is bound in the inner mitochondrial membrane and on the plasma membrane of bacterial species. Energy produced through electron transfer is coupled to the pumping of protons against the electrochemical gradient in order to fuel the proton motive force for the synthesis of most of the ATP in the cell. The three mitochondrial encoded subunits of COX, I, II, and III, are conserved across species and the complete function of subunit III remains unknown. Dicyclohexylcarbodiimide (DCCD) is an inhibitor of function which binds specifically to the conserved Glu-90 residue of subunit III. DCCD modification of COX has been shown to induce a conformational change in subunit III, which inhibits the proton pumping and electron transfer mechanisms occurring in subunit I of the enzyme.This work analyzes the catalytic mechanism and environment of bovine heart and R. sphaeroides COX upon DCCD modification in order to gain insight into the significance of subunit III in the functioning of the enzyme as well as to compare the effects of the modification on catalytic activity. The effect of DCCD modification was also analyzed in both physiological and alkaline environments due to data which showed that bovine heart COX exhibits less inhibition of electron transfer activity at pH values 9.5 and 10.0, while R. sphaeroides COX shows less inhibition at pH values 6.5 and 7.0. Both COX enzymes exhibited a steady biphasic pH dependence for electron transfer activity, suggesting that there are two proton binding sites critical in electron transfer activity. Bovine heart COX displayed an alkaline shift from 8.8±0.2 to 9.3±0.1 at site 2, while R. sphareoides COX displayed an acidic shift from 7.8±0.4 to 7.3±0.4 at site 1. To examine the effects of DCCD modification on the environment of hemes a and a3, the Soret region of the CD spectrum was analyzed. DCCD induced a red shift from 427.7 ± 0.3 nm in control to 428.2 ± 0.1 nm at pH 7.0 in bovine heart COX and from 429.2 ± 0.2 nm to 429.6 ± 0.1 nm at pH 10. In R. sphaeroides, a red shift in the CD spectrum was observed from 429.4 ± 0.1 nm in WT to 430.2 ± 0.1 nm in the DCCD-modified enzyme at pH 7.0 and from 431.5 ± 0.5 nm in WT to 431.9 ± 0.4 nm in DCCD-modified enzyme at pH 10.0. The heme a and a3 environment was also monitored using heme a reduction during steady state electron transfer. Heme a was found to be 18±1% reduced in control bovine heart COX during electron transfer and 33±2% reduced in DCCD-modified COX at pH 7.0 At pH 10.0, control bovine heart COX exhibited a heme a reduction level of 67±7% and DCCD-modified enzyme yielded a reduction level of 93±6%. In0 R. sphaeroides, heme a was found to be 41 ± 2% reduced and DCCD-modified enzyme was 36 ± 2% reduced at pH 7.0. At pH 10.0, WT R. sphaeroides exhibited a heme a reduction level of 33 ± 4% and DCCD-modified enzyme yielded a reduction level of 47 ± 5%. In summary, our results… Advisors/Committee Members: Prochaska, Lawrence (Advisor).

Subjects/Keywords: Biochemistry; Cytochrome c Oxidase; Respiratory enzymes; Dicyclohexylcarbodiimide

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Fisher, K. N. (2014). Investigating the Undefined Role of Subunit IIIin Cytochrome c Oxidase Functioning Using Dicyclohexylcarbodiimide Chemical Modification; Insight Into Enzyme Structure and Molecular Mechanism. (Masters Thesis). Wright State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=wright1405294648

Chicago Manual of Style (16th Edition):

Fisher, Kelli Nicole. “Investigating the Undefined Role of Subunit IIIin Cytochrome c Oxidase Functioning Using Dicyclohexylcarbodiimide Chemical Modification; Insight Into Enzyme Structure and Molecular Mechanism.” 2014. Masters Thesis, Wright State University. Accessed October 28, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=wright1405294648.

MLA Handbook (7th Edition):

Fisher, Kelli Nicole. “Investigating the Undefined Role of Subunit IIIin Cytochrome c Oxidase Functioning Using Dicyclohexylcarbodiimide Chemical Modification; Insight Into Enzyme Structure and Molecular Mechanism.” 2014. Web. 28 Oct 2020.

Vancouver:

Fisher KN. Investigating the Undefined Role of Subunit IIIin Cytochrome c Oxidase Functioning Using Dicyclohexylcarbodiimide Chemical Modification; Insight Into Enzyme Structure and Molecular Mechanism. [Internet] [Masters thesis]. Wright State University; 2014. [cited 2020 Oct 28]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=wright1405294648.

Council of Science Editors:

Fisher KN. Investigating the Undefined Role of Subunit IIIin Cytochrome c Oxidase Functioning Using Dicyclohexylcarbodiimide Chemical Modification; Insight Into Enzyme Structure and Molecular Mechanism. [Masters Thesis]. Wright State University; 2014. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=wright1405294648

2. ΠΑΙΡΑΣ, ΓΙΩΡΓΟΣ. ΣΥΝΘΕΣΗ ΤΡΟΠΟΠΟΙΗΜΕΝΩΝ ΣΤΕΡΟΕΙΔΩΝ ΕΣΤΕΡΩΝ, ΜΕ ΠΑΡΑΓΩΓΑ ΤΗΣ Ν, Ν-ΔΙΣ(2-ΧΛΩΡΟΑΙΘΥΛ)ΑΝΙΛΙΝΗΣ ΚΑΙ ΒΙΟΛΟΓΙΚΗ ΔΡΑΣΗ ΑΥΤΩΝ.

Degree: 1987, Πανεπιστήμιο Πατρών; University of Patras

THE COMPOUNDS HERE PREPARED ARE STEROIDAL ESTERS OF N,N-BIS (2- CHLOROETHYL)ANILI WITH SEVERAL OF THE STEROIDS MODIFIED TO THE A OR D LACTAMS BEFORE ESTERIFICATION. SIXTEEN COMPOUNDS WITH POSSIBLE CYTOSTATIC ACTIVITY WERE PREPARED BY TWODIFFERENT METHODS. THE ALHYLATING AGENTS USED WERE THE MUSTARDS OF PHENYLOCETIC, PHENOXYACETIC, PHENYLBUTYRIC AND BENZOIC ACID RESPECTIVELY, AND THE STEROIDAL ALCOHOLS WERE EPI-ANDROSTERONE, CIS ANDROSTERONE, DEHYDRO-EPI-ANDROSTERONE, TESTOSTERONE, ESTRONE, PREGNENOLONE AND ANDROSTANALONE.

ΟΙ ΕΝΩΣΕΙΣ ΔΠΟΥ ΠΑΡΑΣΚΕΥΑΣΤΗΚΑΝ ΣΤΗΝ ΠΑΡΟΥΣΑ ΕΡΓΑΣΙΑ ΕΙΝΑΙ ΣΤΕΡΟΕΙΔΕΙΣ ΕΣΤΕΡΕΣ ΤΗΣ Ν,Ν-ΔΙΣ(2-ΧΛΩΡΟΑΙΘΥΛ)ΑΝΙΛΙΝΗΣ ΜΕ ΤΑ ΠΕΡΙΣΣΟΤΕΡΑ ΣΤΕΡΟΕΙΔΗ ΤΡΟΠΟΠΟΙΗΜΕΝΑ ΠΡΟΣ ΤΙΣ Α ΚΑΙ D ΛΑΚΤΑΜΕΣ ΠΡΙΝ ΤΗΝ ΕΣΤΕΡΟΠΟΙΗΣΗ. ΔΕΚΑΕΞΙ ΠΡΟΙΟΝΤΑ ΜΕ ΠΙΘΑΝΗ ΚΥΤΤΑΡΟΣΤΑΤΙΚΗ ΔΡΑΣΗ ΠΑΡΑΣΚΕΥΑΣΤΗΚΑΝ ΜΕ ΔΥΟΔΙΑΦΟΡΕΤΙΚΕΣ ΜΕΘΟΔΟΥΣ. ΟΙ ΑΛΚΥΛΙΩΤΙΚΟΙ ΠΑΡΑΓΟΝΤΕΣ ΠΟΥ ΧΡΗΣΙΜΟΠΟΙΗΘΗΚΑΝ ΗΤΑΝ ΟΙ ΜΟΥΣΤΑΡΔΕΣ ΤΟΥ ΦΑΙΝΥΛΟΞΙΚΟΥ, ΦΑΙΝΟΞΥΟΞΙΚΟΥ, ΦΑΙΝΥΛΟΒΟΥΤΥΡΙΚΟΥ ΚΑΙ (Κ- ΒΕΝΖΟΙΚΟΥ ΟΞΕΟΣ, ΕΝΩ ΤΑ ΣΤΕΡΟΕΙΔΗ (ΑΛΚΟΟΛΕΣ) ΗΤΑΝ ΗΕΠΙ- ΑΝΔΡΟΣΤΕΡΟΝΗ, Η CIS-ΑΝΔΡΟΣΤΕΡΟΝΗ, Η ΔΕΥΔΡΟ-ΕΠΙ-ΑΝΔΡΟΣΤΕΡΟΝΗ, Η ΤΕΣΤΟΣΤΕΡΟΝΗ, Η ΟΙΣΤΡΟΝΗ Η ΠΡΕΓΝΕΤΟΞΟΝΗ ΚΑΙ Η ΑΝΔΡΟΣΤΑΝΟΞΟΝΗ.

Subjects/Keywords: Alkylating agents; Chemotherapy; Chlorambucil; DICYCLOHEXYLCARBODIIMIDE {ESTERIFICATION WITH}; MODIFIED STEROIDAL ESTERS; Nitrogen mustards; NOR-STEROID; Omo-aza steroids; PHENOXYACETIC ACID {MUSTARD OF}; PHENYLACETIC ACID {MUSTARD OF}; {ΕΣΤΕΡΟΠΟΙΗΣΗ ΜΕ} ΔΙΚΥΚΛΟΕΞΥΛΚΑΡΙΞΟΔΙΙΜΙΔΙΟ; Αλκυλιωτικοί παράγοντες; ΜΟΥΣΤΑΡΔΑ ΤΟΥ ΦΑΙΝΟΞΥΟΞΙΚΟΥ ΟΞΕΟΣ; ΜΟΥΣΤΑΡΔΑ ΤΟΥ ΦΑΙΝΥΛΟΞΙΚΟΥ ΟΞΕΟΣ; Μουστάρδές αζώτου; ΝΟΡ-ΣΤΕΡΟΕΙΔΕΣ; Ομο αζωτουχα στεροειδή; ΤΡΟΠΟΠΟΙΗΜΕΝΟΙ ΣΤΕΡΟΕΙΔΕΙΣ ΕΣΤΕΡΕΣ; Χημειοθεραπεία; Χλωραμπουκίλη

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

ΠΑΙΡΑΣ, . (1987). ΣΥΝΘΕΣΗ ΤΡΟΠΟΠΟΙΗΜΕΝΩΝ ΣΤΕΡΟΕΙΔΩΝ ΕΣΤΕΡΩΝ, ΜΕ ΠΑΡΑΓΩΓΑ ΤΗΣ Ν, Ν-ΔΙΣ(2-ΧΛΩΡΟΑΙΘΥΛ)ΑΝΙΛΙΝΗΣ ΚΑΙ ΒΙΟΛΟΓΙΚΗ ΔΡΑΣΗ ΑΥΤΩΝ. (Thesis). Πανεπιστήμιο Πατρών; University of Patras. Retrieved from http://hdl.handle.net/10442/hedi/0824

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

ΠΑΙΡΑΣ, ΓΙΩΡΓΟΣ. “ΣΥΝΘΕΣΗ ΤΡΟΠΟΠΟΙΗΜΕΝΩΝ ΣΤΕΡΟΕΙΔΩΝ ΕΣΤΕΡΩΝ, ΜΕ ΠΑΡΑΓΩΓΑ ΤΗΣ Ν, Ν-ΔΙΣ(2-ΧΛΩΡΟΑΙΘΥΛ)ΑΝΙΛΙΝΗΣ ΚΑΙ ΒΙΟΛΟΓΙΚΗ ΔΡΑΣΗ ΑΥΤΩΝ.” 1987. Thesis, Πανεπιστήμιο Πατρών; University of Patras. Accessed October 28, 2020. http://hdl.handle.net/10442/hedi/0824.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

ΠΑΙΡΑΣ, ΓΙΩΡΓΟΣ. “ΣΥΝΘΕΣΗ ΤΡΟΠΟΠΟΙΗΜΕΝΩΝ ΣΤΕΡΟΕΙΔΩΝ ΕΣΤΕΡΩΝ, ΜΕ ΠΑΡΑΓΩΓΑ ΤΗΣ Ν, Ν-ΔΙΣ(2-ΧΛΩΡΟΑΙΘΥΛ)ΑΝΙΛΙΝΗΣ ΚΑΙ ΒΙΟΛΟΓΙΚΗ ΔΡΑΣΗ ΑΥΤΩΝ.” 1987. Web. 28 Oct 2020.

Vancouver:

ΠΑΙΡΑΣ . ΣΥΝΘΕΣΗ ΤΡΟΠΟΠΟΙΗΜΕΝΩΝ ΣΤΕΡΟΕΙΔΩΝ ΕΣΤΕΡΩΝ, ΜΕ ΠΑΡΑΓΩΓΑ ΤΗΣ Ν, Ν-ΔΙΣ(2-ΧΛΩΡΟΑΙΘΥΛ)ΑΝΙΛΙΝΗΣ ΚΑΙ ΒΙΟΛΟΓΙΚΗ ΔΡΑΣΗ ΑΥΤΩΝ. [Internet] [Thesis]. Πανεπιστήμιο Πατρών; University of Patras; 1987. [cited 2020 Oct 28]. Available from: http://hdl.handle.net/10442/hedi/0824.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

ΠΑΙΡΑΣ . ΣΥΝΘΕΣΗ ΤΡΟΠΟΠΟΙΗΜΕΝΩΝ ΣΤΕΡΟΕΙΔΩΝ ΕΣΤΕΡΩΝ, ΜΕ ΠΑΡΑΓΩΓΑ ΤΗΣ Ν, Ν-ΔΙΣ(2-ΧΛΩΡΟΑΙΘΥΛ)ΑΝΙΛΙΝΗΣ ΚΑΙ ΒΙΟΛΟΓΙΚΗ ΔΡΑΣΗ ΑΥΤΩΝ. [Thesis]. Πανεπιστήμιο Πατρών; University of Patras; 1987. Available from: http://hdl.handle.net/10442/hedi/0824

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.