18.3 part 2
18.3 part 3
18.3 part 4
18.3 part 5
18.3 part 6
100

What are the prosthetic groups, matrix side, and membrane core of C1?  

FMN, Fe-S

NADH

Q

100

What happens to the e- donated by NADH and FADH2? 

They are passed to e- carriers in protein complexes

100

What are iron-sulfur proteins, what do they do and how do they cycle?

nonheme iron proteins 

prominant e- carriers

cycle between Fe2+ and Fe3+ as they donate and accept e-

100

Where is succinate dehydrogenase of the CAC found?

Complex 2

100

What are the steps and characteristics of the Q-cycle?

1st half: 1 e- of QH2 reduces cytochrome c and yields Q.-

2nd half: another e- reduces cytochrome c and Q.-

4 protons pumped in 1 cycle

deficiency --> pathological condition 

200

What are the prosthetic groups, matrix side and membrane core of C2?

FAD, Fe-S

Succinate

Q

200

What are the characteristics of coenzyme Q?

Derived from isoprene

Bind + and e-

exist in many oxidation states 

200

What is Frataxin, what can a deficiency lead to and what does it impact?

A small mitochondrial protein that is necessary for Fe-S synthesis

deficiency leads to Friedrich's ataxia

causes issue in NS, cardio, skeletal 

200

What is the function of FADH2 from the CAC?

reduce Q --> QH2, which then enter Q pool

200

What does cytochrome C oxidase do and what are the characteristics?

reduces oxygen to water

donates 4 e- from 4 molecules for reduction

during the rxn 8 protons are removed from the matrix, 4 are chemical protons used to reduce oxygen and 4 are pumped into the intermembrane space 

300

What are the prosthetic groups, intermembrane side, and membrane core of C3?

Heme BH, BL, C, Fe-s

Cytochrome C

Q

300

What is present in the Q pool and where is the Q pool located?

oxidized and reduced Q

inner mitochondrial membrane 

300

How are e- from NADH passed and where do they end up?

Q --> QH2 by complex 1

QH2 goes to Q pool 

300

What is the function of e- from QH2 and where does it function?

reduces 2 molecule of cytochrome C at complex 3

300

What are the subunits of cytochrome C oxidase and how do they flow?

2 heme (a, a3)

2 copper (CuA - 2 copper ions, CuB - 3 histine residues, 1 is covalently bonded to tyrosine)

2 e- flow from cytochrome c --> CuA/CuA --> heme a --> a3 --> CuB


400
What are the prosthetic groups and intermembrane side of C4?

Heme a, a3, CuA, CuB

Cytochrome C

400

What is cytochrome C and what does it do?

An e- carrier that employs an iron incorporated into a heme 

carries e- from C3 --> C4

400

What are the e- carriers between NADH and Q and what happens at this complex? 

FMN and iron proteins

4 protons are pumped out of the matrix by complex 1

400

What are the cytochromes at complex 3

Cytochrome B and C1

400

What happens when the Fe of heme a3 and CuB are reduced?

They bind to oxygen and a peroxide bridge forms between them 

500

How does heme iron cycle?

Between Fe2+ and Fe3+ as it donates and accepts e- 

500

What is the function of ubiquinol?

The entry point for e- from FADH2 of flavoproteins

500

What does the Q cycle do?

funnels e- from 2 e- carrier to 1 e- carrier and pumps proteins

QH2 --> 2 e- carrier

Cytochrome C --> 1 e- carrier

500

What is the mechanism of cytochrome C oxidase?

1. Fe of heme a3 and CuB are reduced by 2 molecules of cytochrome c 

2. heme a3 and CuB bind to O2 forming peroxide bridge 

3. 2 e- and 2 protons come in and cleave bridge 

4. 2 more protons come in and release water 

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