Microbiology Chapter 10

What is metabolism?

the total of all chemical reactions in the cell

Which provides energy: catabolism or anabolism?

catabolism

Which consists of fueling reactions: catabolism or anabolism?

catabolism

Which synthesizes complex organic molecules: catabolism or anabolism?

anabolism

How many steps in the nitrogen cycle are solely done by microbes?

4 of 8

1 calorie equals how many joules?

4.2

How many phosphates in ATP have high energy bonds?

2

List the four types of RNA nucleotides.

ATP, GTP, UTP, CTP

ATP has a high _________ __________ potential.

phosphate transfer

A phosphorylated compound is considered "high energy" if it releases ____ kJ/mol or more.

30

Electron donor and acceptor are a __________ ________ pair

conjugate redox

As you move down the half reaction table, reducing power _________.

decreases

Which half reaction is flipped: the one donating electrons/being oxidized/reducing agent or the one accepting electrons/being reduced/oxidizing agent?

the one donating electrons/being oxidized/reducing agent

What is Faraday's constant, in kcal/volt?

23

What is Faraday's constant, in kJ/volt?

96.5

In the Nernst equation, free energy change equals:

-nFE

In the Nernst equation, E is equal to the E of the ______ agent minus E of the ________ agent

oxidizing, reducing

In the ETC, the first electron carrier has the most __________ E.

negative

In the ETC, what do NADH and NADPH do?

Accept two electrons and one proton

In the ETC, what do FAD and FMN do? Give an example.

Carry two electrons and two protons, flavoproteins

In the ETC, what does coQ/ubiquinone do? Is coQ a protein?

Transports two electrons and two protons, no it is a lipid

What do cytochromes do?

use iron to transfer one electron at a time

What do nonheme iron-sulfur proteins do? Give an example.

use iron to transport one electron at a time, ferredoxin

Name two components of complex II in the ETC

flavoprotein, iron protein

The polypeptide(s) (apoenzyme) and the nonprotein components (cofactor) come together to form what?

holoenzyme

Name two ways in which enzymes lower the activation energy of a reaction.

increasing concentrations of substrates at active site, orienting substrates properly

Name three things that effect enzyme activity.

substrate concentration, pH, temperature

What type of inhibitor blocks substrate binding?

competitive

What type of inhibitor allows substrate to bind, but blocks reaction?

noncompetitive

Give three examples of the role of ribozymes.

catalyze peptide bond formation, self-splicing, involved in self-replication

Name the three major mechanisms of regulating metabolism.

compartmentation, transcriptional/translational, post-translational

What does an allosteric effector do? Is it reversible or irreversible?

binds to a site on the enzyme that is not the active site, reversible

What is the term for the site in which an allosteric effector binds?

regulatory site

A positive allosteric effector turns the enzyme _____ when bound.

on

A negative allosteric effector turns the enzyme ____ when bound.

off

Is covalent modification of enzymes reversible or irreversible?

reversible

What does the pacemaker enzyme do?

decides how fast the reaction will occur

In feedback inhibition, each end-product can regulate what two things?

its own branch, initial pacemaker enzyme