Nitrogen 1 Flashcards

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1
Q

What do amino acids and nucleotides contain that carbohydrates and fats don’t?

A

Nitrogen

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2
Q

Where does the nitrogen in our bodies come from?

A

Our diet

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3
Q

How do the plants/animals we eat get their nitrogen?

A

From nitrogen fixing bacteria known as diazotrophs

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4
Q

What are the 3 stages called in the nitrogen cycle?

A

Fixation

Assimilation

Degreadation

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5
Q

What is the structure of nitrogen?

A

2 nitrogen atoms are held together by triple bond making it very unreactive

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6
Q

How can nitrogen be captured?

A

Adding oxygen using lightening to form NO or NO

Adding hydrogen using the Haber process to form NH3

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7
Q

What are 2 examples of nitrogen-fixing bacteria?

A
  • Cyanobacteria found in Lake Atitlan

- Rhizobium bacteria found on root nodules of legumes

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8
Q

What do bacteria require for nitrogen fixation?

A

Energy

Nitrogenase enzymes

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9
Q

What does the fixation of nitrogen produce?

A

Un-ionised ammonia (NH3) which in water will exist in equilibrium with ionised ammonium (NH4+)

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10
Q

What inactivates nitrogenase?

A

Oxygen

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11
Q

How do nitrogen fixing bacteria get around the abundance of oxygen?

A

They live anaerobically

Some uncouple mitochondria which increases electron flow and ‘burns’ off oxygen in the cell

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12
Q

How do cyanobacteria prevent O2 entry?

A

They form heterocysts whose cell wall prevents oxygen entry

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13
Q

How do leguminous plants allow nitrogenase to work?

A

They produce leghaemoglobin which binds oxygen and keeps the concentration low enough to allow nitrogenase to remain activated and work

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14
Q

What happens after nitrogen is fixed?

A

Soil bacteria convert ammonia to nitrite and then to nitrate (nitrification).
Nitrate is then taken up by plants and microbes.
Once the nitrate has been taken up, it is then converted back to ammonia via nitrite

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15
Q

What is the only amino acid that can obtain its nitrogen directly from NH4 and the only one which can give it up directly?

A

Glutamate

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16
Q

What are the 4 amino acids which are found in higher concentration in cells compared to other amino acids

A
  • Alanine
  • Glutamine
  • Glutamate
  • Aspartate
17
Q

What are the roles of glutamate?

A
  • Excitatory neurotransmitters
  • Important in taste
  • Amino acid breakdown
18
Q

What is transamination?

A

Conservation of nitrogen by transferring amino groups between different molecules

19
Q

What are the general principles of transamination?

A
  • No loss or gain of nitrogen
  • Readily reversible
  • One of the 2 substrate pairs is often glutamate
  • Amino acid 1+ Keto acid 2= Keto acid 1+ Amino acid 2
20
Q

What is the difference between an amino acid and a a-keto acid?

A
  • Amino acid has an NH3 group attached to a carbon which is attached to a COOH group
  • a-Keto acid has a C double bond O attached to the acidic group
21
Q

What does the reversible nature of transamination allow it to do?

A

Participate in amino acid synthesis and degradation

22
Q

What do all aminotransferases rely on?

A

Pyridoxal phosphate cofactor

23
Q

What typically accepts amino groups?

A

a-ketoglutarate

24
Q

What acts as a temporary storage of nitrogen?

A

L-glutamine

25
Q

What can L-glutamine do?

A

Donate the amino group when needed for amino acid biosynthesis

26
Q

What is pyridoxal phosphate?

A

-Cofactor made from vitamin B6

27
Q

What does pyridoxal phosphate do?

A

Transfers the amino group during the reaction

28
Q

What does the presence of aminotransferases in the plasma indicate?

A

Cell damage as they are intracellular proteins

29
Q

What aminotransferases are particularly good indicators of cell damage

A
  • Aspartate aminotransferases (aspartate to oxaloacetate)

- Alanine aminotransferases (alanine to pyruvate)

30
Q

How is liver disease monitored?

A

Measuring serum levels of alanine aminotransferase or aspartate aminotransferase

31
Q

What is a significant energy yielding pathway in carnivores?

A

Oxidation of amino acids

32
Q

Where do micro-organisms get their nitrogen from?

A

Scavenged from their environment for fuel

33
Q

What are the 3 circumstances that amino acids undergo oxidative catabolism?

A
  • Leftover amino acids from normal protein turnover are degraded
  • Dietary amino acids that exceed body’s protein synthesis needs are degraded
  • Proteins in the body are broken down to supply amino acids for catabolism when carbohydrates are in short supply